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cis-zeatin + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
cis-zeatin + acceptor + H2O
?
cis-zeatin + electron acceptor
(2Z)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
cis-zeatin + oxidized 2,6-dichlorophenolindophenol
?
cis/trans-zeatin + FAD + H2O
adenine + ? + FADH2
cis/trans-zeatin riboside + FAD + H2O
adenine + ? + FADH2
-
-
-
ir
cytokinin + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
? + reduced 2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
-
-
?
cytokinin riboside + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
? + reduced 2,3-dimethoxy-5-methyl-1,4-benzoquinone
-
-
-
?
dihydrozeatin + electron acceptor
?
-
-
-
-
?
isopentenyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
isopentenyladenine 9-glucoside + 2,6-dichlorophenolindophenol
adenine 9-glucoside + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
isopentenyladenosine + 2,6-dichlorophenolindophenol
adenosine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
isopentenyladenosine + acceptor + H2O
? + reduced acceptor
isopentenyladenosine monophosphate + 2,6-dichlorophenolindophenol
adenosine monophosphate + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
kinetin + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
?
-
-
-
?
kinetin + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
low activity
-
-
?
kinetin + electron acceptor
2-furaldehyde + adenine + reduced electron acceptor
-
-
-
-
?
kinetin + FAD
2-furaldehyde + adenine + FADH2
-
-
-
-
?
kinetin riboside + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
?
-
-
-
?
m-topolin + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
very low activity
-
-
?
N-benzyladenine + electron acceptor
benzaldehyde + adenine + reduced electron acceptor
-
-
-
-
?
N-methyl-isopentenyladenine + FAD
?
-
-
-
-
?
N6-(2-butynyl)adenine + 2,6-dichlorophenol indophenol
?
very effective electron acceptor
-
-
?
N6-(2-isopentenyl)adenine + 1,4-naphthoquinone
?
-
very effective electron acceptor
-
-
?
N6-(2-isopentenyl)adenine + 1,4-naphthoquinone
adenine + 3-methylbut-2-enal + reduced 1,4-naphthoquinone
-
-
-
?
N6-(2-isopentenyl)adenine + 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) radical + H2O
adenine + 3-methylbut-2-enal + ?
-
-
-
-
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
adenine + 3-methylbut-2-enal + reduced 2,3-dimethoxy-5-methyl-1,4-benzoquinone
i.e. coenzyme Q0
-
-
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
adenine + 3-methylbut-2-enal + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
-
4-nitrosoresorcinol-1-monomethyl ether serves as a weak electron acceptor of CKX
-
-
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenol indophenol
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
N6-(2-isopentenyl)adenine + 4-nitrosoresorcinol-1-monomethyl ether + H2O
adenine + 3-methylbut-2-enal + reduced 4-nitrosoresorcinol-1-monomethyl ether
-
4-nitrosoresorcinol-1-monomethyl ether serves as a weak electron acceptor of CKX
-
-
?
N6-(2-isopentenyl)adenine + acceptor + H2O
?
-
preferred substrate of isozyme AtCKX4
-
-
?
N6-(2-isopentenyl)adenine + caffeic acid
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + coenzyme Q1
adenine + 3-methylbut-2-enal + reduced coenzyme Q1
-
-
-
?
N6-(2-isopentenyl)adenine + CuCl2
?
N6-(2-isopentenyl)adenine + CuCl2 + H2O
adenine + 3-methylbut-2-enal + ?
N6-(2-isopentenyl)adenine + cytochrome c
adenine + 3-methylbut-2-enal + reduced cytochrome c
-
-
-
?
N6-(2-isopentenyl)adenine + daphnoretin
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + duroquinone
?
-
low activity
-
-
?
N6-(2-isopentenyl)adenine + electron acceptor
adenine + 3-methylbut-2-enal + reduced electron acceptor
-
-
-
-
?
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
N6-(2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
ir
N6-(2-isopentenyl)adenine + hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one + H2O
adenine + 3-methylbut-2-enal + reduced hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one
-
CKX1 is able to use hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one as a poor electron acceptor at neutral pH levels, but not in acidic pH levels
-
-
?
N6-(2-isopentenyl)adenine + o-coumaric acid
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + O2
?
-
low activity
-
-
?
N6-(2-isopentenyl)adenine + O2
adenine + 3-methylbut-2-enal + H2O2
oxidative degradation of cytokinins, slow reaction, low substrate specificity
-
-
?
N6-(2-isopentenyl)adenine + plantacyanine
adenine + 3-methylbut-2-enal + reduced plantacyanine
electron acceptor from spinach
-
-
?
N6-(2-isopentenyl)adenine + potassium ferricyanide
?
-
low activity
-
-
?
N6-(2-isopentenyl)adenine + rosmarinic acid
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + scopoletin
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + spinach plantacyanine
adenine + 3-methylbut-2-enal + reduced spinach plantacyanine
-
-
-
r
N6-(2-isopentenyl)adenine + vitamin K1
adenine + 3-methylbut-2-enal + reduced vitamin K1
-
-
-
?
N6-(2-isopentenyl)adenine + vitamin K3
?
-
low activity
-
-
?
N6-(2-isopentenyl)adenine + vitamin K3
adenine + 3-methylbut-2-enal + reduced vitamin K3
-
-
-
?
N6-(2-isopentenyl)adenine 9-beta-D-glucoside + 3',5'-dimethoxy-4'-hydroxyacetophenone + H2O
adenine 9-beta-D-glucoside + 3-methylbut-2-enal + ?
i.e. iP9G, best substrate for isozyme AtCKX1 at pH 5.0, 3',5'-dimethoxy-4-hydroxyacetophenone is the best acceptor
-
-
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + 2,3,5-triphenyl-tetrazolium chloride + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + 3',5'-dimethoxy-4'-hydroxyacetophenone + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + ferricyanide + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ferrocyanide
-
-
-
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + ferricytochrome c + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ferrocytochrome c
-
-
-
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + NAD+ + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + O2 + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + oxidized 2,6-dichlorophenolindophenol + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside 5'-phosphate + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
adenine 9-beta-D-riboside 5'-phosphate + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine 9-glucoside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
low activity
-
-
?
N6-(2-isopentenyl)adenine 9-riboside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
N6-(2-isopentenyl)adenine 9-riboside-5'-monophosphate + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
low activity
-
-
?
N6-(2-isopentenyl)adenose + 2,6-dichlorophenolindophenol
adenosine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
N6-(2-isopentenyl)adenosine + 2,6-dichlorophenol indophenol
?
very effective electron acceptor
-
-
?
N6-(2-isopentenyl)adenosine + FAD
adenosine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(4-hydroxy-2-butynyl)adenine + 2,6-dichlorophenol indophenol
?
very effective electron acceptor
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,3-dimetoxy-5-methyl-1,4-benzoquinone + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
N6-(DELTA2-isopentenyl)adenine + 4-methylcatechol + H2O
adenine + 3-methylbut-2-enal + reduced 4-methylcatechol
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + acetosyringone + H2O
adenine + 3-methylbut-2-enal + reduced acetosyringone
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + CuCl2 + H2O
adenine + 3-methyl-2-butenal + CuCl + Cl-
-
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
N6-(DELTA2-isopentenyl)adenine + guaiacol + H2O
adenine + 3-methylbut-2-enal + reduced guaiacol
-
-
-
?
N6-(DELTA2-isopentenyl)adenine-9-beta-D-glucoside + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + 2,6-dichlorophenolindophenol + H2O
adenosine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
artificial electron acceptor
-
-
?
N6-(DELTA2-isopentenyl)adenosine + 4-methylcatechol + H2O
adenosine + 3-methylbut-2-enal + reduced 4-methylcatechol
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + acetosyringone + H2O
adenosine + 3-methylbut-2-enal + reduced acetosyringone
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
N6-(DELTA2-isopentenyl)adenosine + guaiacol + H2O
adenosine + 3-methylbut-2-enal + reduced guaiacol
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine-5'-monophosphate + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-benzyladenine + electron acceptor
?
-
-
-
-
?
N6-benzyladenine + FAD + H2O
adenine + ? + FADH2
N6-dimethylallyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
i.e. isopentenyladenine, reaction via an imine intermediate
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
N6-dimethylallyladenine + FAD + H2O2
adenine + 3-methylbut-2-enal + FADH2 + O2
-
i.e. isopentenyladenine
-
-
?
N6-dimethylallyladenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
i.e. isopentenyladenosine
-
-
ir
N6-hexyladenine + electron acceptor
hexanal + adenine + reduced electron acceptor
-
-
-
-
?
N6-isopentenyl-2-(2-hydroxyethylamino)-9-methyladenine + electron acceptor
3-methyl-2-butenal + 2-hydroxyethylamino-9-methyladenine + reduced electron acceptor
-
-
-
-
?
N6-isopentenyl-2-methylthioadenine + electron acceptor
3-methyl-2-butenal + 2-methylthioadenine + reduced electron acceptor
-
-
-
-
?
N6-isopentenyladenine + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
?
-
-
-
?
N6-isopentenyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methyl-2-butenal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-isopentenyladenine + CuCl2
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced dichlorophenolindophenol
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
N6-isopentenyladenine + oxidized 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
N6-isopentenyladenine 9-beta-D-glucoside + oxidized 2,6-dichlorophenolindophenol
adenine 9-beta-D-glucoside + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-isopentenyladenine-9-beta-D-glucoside + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
?
-
-
-
?
N6-isopentenyladenosine + 2,6-dichlorophenolindophenol
3-methylbut-2-enal + adenosine + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-isopentenyladenosine + electron acceptor
3-methylbut-2-enal + adenosine + reduced electron acceptor
N6-isopentenyladenosine + oxidized 2,6-dichlorophenolindophenol
adenosine + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-methyl-isopentenyladenine + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
very low activity
-
-
?
O-beta-D-glucosyl-trans-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
-
-
?
o-topolin + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
very low activity
-
-
?
p-topolin + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
very low activity
-
-
?
p-topolin + FAD
?
-
-
-
-
?
thidiazuron + electron acceptor
?
-
-
-
-
?
trans-zeatin + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
?
-
-
-
?
trans-zeatin + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
very effective substrate
-
-
?
trans-zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
cis-zeatin is utilized only by some tissue-specific forms but not by HvCKX2
-
-
?
trans-zeatin + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
trans-zeatin + acceptor + H2O
?
trans-zeatin + electron acceptor
(2E)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
-
-
-
?
trans-zeatin + FAD + H2O
? + FADH2
trans-zeatin + FAD + H2O
adenine + ? + FADH2
trans-zeatin + oxidized 2,6-dichlorophenolindophenol
?
trans-zeatin 9-glucoside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
low activity
-
-
?
trans-zeatin 9-riboside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
very effective substrate
-
-
?
trans-zeatin O-glucoside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
trans-zeatin riboside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
trans-zeatin riboside + 2,6-dichlorophenolindophenol + H2O
?
most favorable substrate
-
-
?
trans-zeatin riboside O-glucoside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
trans-zeatin ribotide + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
trans-zeatin-9-glucoside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
zeatin + 2,6-dichlorophenolindophenol
4-hydroxy-3-methylbut-2-enal + adenine + reduced 2,6-dichlorophenolindophenol
-
-
-
?
zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
zeatin + FAD
? + FADH2
-
-
-
?
zeatin + FAD + H2O
adenine + 4-hydroxy-3-methylbut-2-enal + FADH2
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
zeatin riboside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
additional information
?
-
cis-zeatin + acceptor + H2O
?
-
-
-
-
?
cis-zeatin + acceptor + H2O
?
-
preferred substrate of isozyme ZmCKX10
-
-
?
cis-zeatin + electron acceptor
(2Z)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
-
-
-
?
cis-zeatin + electron acceptor
(2Z)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
-
-
-
?
cis-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
-
-
-
?
cis-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
-
-
?
cis/trans-zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
ir
cis/trans-zeatin + FAD + H2O
adenine + ? + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
isopentenyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
isopentenyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
isopentenyladenosine + acceptor + H2O
? + reduced acceptor
-
-
-
-
?
isopentenyladenosine + acceptor + H2O
? + reduced acceptor
-
-
-
-
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
-
-
-
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
-
-
-
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenol indophenol
?
-
very effective electron acceptor
-
-
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenol indophenol
?
-
very effective electron acceptor
-
-
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenol indophenol
?
-
-
-
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenol indophenol
?
very effective electron acceptor
-
-
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-(2-isopentenyl)adenine + CuCl2
?
-
-
-
?
N6-(2-isopentenyl)adenine + CuCl2
?
-
low activity
-
-
?
N6-(2-isopentenyl)adenine + CuCl2
?
-
-
-
-
?
N6-(2-isopentenyl)adenine + CuCl2 + H2O
adenine + 3-methylbut-2-enal + ?
-
-
-
-
?
N6-(2-isopentenyl)adenine + CuCl2 + H2O
adenine + 3-methylbut-2-enal + ?
-
-
-
-
?
N6-(2-isopentenyl)adenine + CuCl2 + H2O
adenine + 3-methylbut-2-enal + ?
-
-
-
-
?
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
the natural terminal electron acceptor probably is a p-quinone or a similar compound, high substrate specificity for N6-(2-isopentenyl)adenine
-
-
?
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
-
formation of a binary enzyme-product complex between the cytokinin imine and the reduced enzyme. The binary complex of the reduced enzyme and imine product intermediate decays relatively slowly to form an unbound product, cytokinin imine, which accumulates in the reaction mixture
-
-
?
N6-(2-isopentenyl)adenine 9-riboside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
-
-
-
?
N6-(2-isopentenyl)adenine 9-riboside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
preferred substrate
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
artificial electron acceptor
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
artificial electron acceptor
-
-
?
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
-
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
oxidative degradation of cytokinins
-
-
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-benzyladenine + FAD + H2O
adenine + ? + FADH2
-
-
-
-
ir
N6-benzyladenine + FAD + H2O
adenine + ? + FADH2
substrate binding mechanism and structure, overview
-
-
ir
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
i.e. isopentenyladenine
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
i.e. isopentenyladenine
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
i.e. isopentenyladenine
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
i.e. isopentenyladenine
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
i.e. isopentenyladenine
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Phaseolus sp.
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Phaseolus sp.
-
i.e. isopentenyladenine
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
i.e. isopentenyladenine
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
-
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
i.e. isopentenyladenine
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
FAD is cofactor
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
FAD is cofactor
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
FAD is cofactor
-
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
-
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
oxidative degradation
-
-
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
substrate binding mechanism and structure, overview
-
-
ir
N6-isopentenyladenine + oxidized 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
N6-isopentenyladenine + oxidized 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-isopentenyladenosine + electron acceptor
3-methylbut-2-enal + adenosine + reduced electron acceptor
-
-
-
-
?
N6-isopentenyladenosine + electron acceptor
3-methylbut-2-enal + adenosine + reduced electron acceptor
-
-
-
-
?
N6-isopentenyladenosine + electron acceptor
3-methylbut-2-enal + adenosine + reduced electron acceptor
-
-
-
-
?
trans-zeatin + acceptor + H2O
?
-
-
-
-
?
trans-zeatin + acceptor + H2O
?
-
preferred substrate of isozymes AtCKX4 and AtCKX1
-
-
?
trans-zeatin + acceptor + H2O
?
-
-
-
-
?
trans-zeatin + acceptor + H2O
?
-
preferred substrate of isozymes ZmCKX1 and ZmCKX10
-
-
?
trans-zeatin + FAD + H2O
? + FADH2
-
-
-
-
ir
trans-zeatin + FAD + H2O
? + FADH2
substrate binding mechanism and structure, overview
-
-
ir
trans-zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
ir
trans-zeatin + FAD + H2O
adenine + ? + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
trans-zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
-
?
trans-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
-
-
-
?
trans-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
-
-
?
zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
-
-
ir
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
-
-
-
?
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
-
-
-
?
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
-
-
-
?
zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
Phaseolus sp.
-
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
Phaseolus sp.
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin riboside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
zeatin riboside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
additional information
?
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
the free bases and their ribosides are the preferred substrates
-
-
?
additional information
?
-
-
the free bases and their ribosides are the preferred substrates
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, by controlling the cytokinin level enzyme controls proliferation and differentiation of plant cells
-
-
?
additional information
?
-
-
AtCKX2 prefers p-quinones and 2,6-dichlorophenol indophenol as electron acceptors, low reactivity with oxygen
-
-
?
additional information
?
-
-
no activity with dihydrozeatin
-
-
?
additional information
?
-
-
no activity with vitamin K1 as electron acceptor
-
-
?
additional information
?
-
-
acceptor and substrate specificity, overview. The enzyme catalyzes the irreversible cleavage of N6-side chains from cytokinins. CKXs also show low cytokinin oxidase activity, but molecular oxygen is a comparatively poor electron acceptor. Vacuolar AtCKX enzymes in certain conditions degrade N6-(2-isopentenyl)adenine di- and triphosphates two to 5times more effectively than its monophosphate
-
-
?
additional information
?
-
acceptor and substrate specificity, overview. The enzyme catalyzes the irreversible cleavage of N6-side chains from cytokinins. CKXs also show low cytokinin oxidase activity, but molecular oxygen is a comparatively poor electron acceptor. Vacuolar AtCKX enzymes in certain conditions degrade N6-(2-isopentenyl)adenine di- and triphosphates two to 5times more effectively than its monophosphate
-
-
?
additional information
?
-
acceptor and substrate specificity, overview. The enzyme catalyzes the irreversible cleavage of N6-side chains from cytokinins. CKXs also show low cytokinin oxidase activity, but molecular oxygen is a comparatively poor electron acceptor. Vacuolar AtCKX enzymes in certain conditions degrade N6-(2-isopentenyl)adenine di- and triphosphates two to 5times more effectively than its monophosphate
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
analysis of enzyme activity regulation
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes
-
-
?
additional information
?
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
tissue and isozyme-specific substrate specificity
-
-
?
additional information
?
-
tissue and isozyme-specific substrate specificity
-
-
?
additional information
?
-
tissue and isozyme-specific substrate specificity
-
-
?
additional information
?
-
tissue and isozyme-specific substrate specificity
-
-
?
additional information
?
-
-
tissue and isozyme-specific substrate specificity, recombinant HvCKX2 prefers cytokinin ribosides as substrates
-
-
?
additional information
?
-
tissue and isozyme-specific substrate specificity, recombinant HvCKX2 prefers cytokinin ribosides as substrates
-
-
?
additional information
?
-
tissue and isozyme-specific substrate specificity, recombinant HvCKX2 prefers cytokinin ribosides as substrates
-
-
?
additional information
?
-
tissue and isozyme-specific substrate specificity, recombinant HvCKX2 prefers cytokinin ribosides as substrates
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
endogenous cytokinin levels after induction with N6-benzylaminopurine, overview, apoplastic enzyme degradation pathway
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
cytokinins stimulate pigment formation and nitrogen fixation
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
reduced expression of OsCKX2 causes cytokinin accumulation in inflorescence meristems and increases the number of reproductive organs, resulting in enhanced grain yield
-
-
?
additional information
?
-
Phaseolus sp.
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
no activity with zeatin, zeatin riboside, or N6-(2-hydroxybenzyl)adenine
-
-
?
additional information
?
-
-
enzyme expression changes differently due to stress response in the 2 pea cultivars
-
-
?
additional information
?
-
-
involvement of cytokinin oxidase/dehydrogenase in regulation of cytokinin levels in leaves
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, results suggest that CKX is responsible for the changes in endogenous cytokinin pool in gibberellic acid-treated plants and most probably this enzyme represents an important link in gibberellic acid/cytokinin cross talk
-
-
?
additional information
?
-
-
effects of exogenously applied auxins on cytokinin levels in seedlings, overview, exogenously applied cytokinins increase the glycosylation level of endogenous cytokinins, overview
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes during infection, cytokinins are involved in pathogenesis
-
-
?
additional information
?
-
enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
-
-
?
additional information
?
-
-
enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
-
-
?
additional information
?
-
enzyme has a major role in control of cytokinin plant hormone levels
-
-
?
additional information
?
-
-
enzyme has a major role in control of cytokinin plant hormone levels
-
-
?
additional information
?
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
specificity for electron acceptors, overview
-
-
?
additional information
?
-
-
specificity for electron acceptors, overview
-
-
?
additional information
?
-
substrate specificity with cytokinins, overiew
-
-
?
additional information
?
-
-
substrate specificity with cytokinins, overiew
-
-
?
additional information
?
-
the substrate binding site is located at amino acid residues 245-491
-
-
?
additional information
?
-
-
the substrate binding site is located at amino acid residues 245-491
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, important for the regulation of early development of the plant embryo
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, important for the regulation of early development of the plant embryo
-
-
?
additional information
?
-
-
laccase and peroxidase catalyze oxidative cleavage of hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one (DIMBOA) to 4-nitrosoresorcinol-1-monomethyl ether (coniferron) which serves as a weak electron acceptor of CKX1. The oxidation of DIMBOA and coniferron generates transitional free radicals that are used by CKX1 as effective electron acceptors. hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-glucoside is not active as an electron acceptor for isozyme CKX1
-
-
?
additional information
?
-
adenosine, abscisic acid, gibberellic acid, and cis-zeatin riboside are no substrates, nor is the reduced dihydrozeatin. Aromatic cytokinins, kinetin and N6-benzyladenine, and the synthetic substituted urea cytokinin thidiazuron are also inactive, as are most cytokinin glucosides and the monophosphate N6-(DELTA2-isopentenyl)adenosine-5'-monophosphate
-
-
?
additional information
?
-
-
adenosine, abscisic acid, gibberellic acid, and cis-zeatin riboside are no substrates, nor is the reduced dihydrozeatin. Aromatic cytokinins, kinetin and N6-benzyladenine, and the synthetic substituted urea cytokinin thidiazuron are also inactive, as are most cytokinin glucosides and the monophosphate N6-(DELTA2-isopentenyl)adenosine-5'-monophosphate
-
-
?
additional information
?
-
enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
-
-
?
additional information
?
-
specificity for electron acceptors, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cis-zeatin + acceptor + H2O
?
-
-
-
-
?
cis/trans-zeatin + FAD + H2O
adenine + ? + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
the natural terminal electron acceptor probably is a p-quinone or a similar compound, high substrate specificity for N6-(2-isopentenyl)adenine
-
-
?
N6-(2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
oxidative degradation
-
-
ir
trans-zeatin + acceptor + H2O
?
trans-zeatin + FAD + H2O
adenine + ? + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
-
-
ir
zeatin + FAD + H2O
adenine + 4-hydroxy-3-methylbut-2-enal + FADH2
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
additional information
?
-
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
oxidative degradation of cytokinins
-
-
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Phaseolus sp.
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
-
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
trans-zeatin + acceptor + H2O
?
-
-
-
-
?
trans-zeatin + acceptor + H2O
?
-
-
-
-
?
zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
Phaseolus sp.
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
additional information
?
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, by controlling the cytokinin level enzyme controls proliferation and differentiation of plant cells
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
analysis of enzyme activity regulation
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes
-
-
?
additional information
?
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
endogenous cytokinin levels after induction with N6-benzylaminopurine, overview, apoplastic enzyme degradation pathway
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
cytokinins stimulate pigment formation and nitrogen fixation
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
reduced expression of OsCKX2 causes cytokinin accumulation in inflorescence meristems and increases the number of reproductive organs, resulting in enhanced grain yield
-
-
?
additional information
?
-
Phaseolus sp.
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
-
enzyme expression changes differently due to stress response in the 2 pea cultivars
-
-
?
additional information
?
-
-
involvement of cytokinin oxidase/dehydrogenase in regulation of cytokinin levels in leaves
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, results suggest that CKX is responsible for the changes in endogenous cytokinin pool in gibberellic acid-treated plants and most probably this enzyme represents an important link in gibberellic acid/cytokinin cross talk
-
-
?
additional information
?
-
-
effects of exogenously applied auxins on cytokinin levels in seedlings, overview, exogenously applied cytokinins increase the glycosylation level of endogenous cytokinins, overview
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes during infection, cytokinins are involved in pathogenesis
-
-
?
additional information
?
-
enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
-
-
?
additional information
?
-
-
enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
-
-
?
additional information
?
-
enzyme has a major role in control of cytokinin plant hormone levels
-
-
?
additional information
?
-
-
enzyme has a major role in control of cytokinin plant hormone levels
-
-
?
additional information
?
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, important for the regulation of early development of the plant embryo
-
-
?
additional information
?
-
-
irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, important for the regulation of early development of the plant embryo
-
-
?
additional information
?
-
enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.004 - 0.009
(2,6-dichloro-pyridin-4-yl)-carbamic acid benzyl ester
0.0002 - 0.039
(2-chloro-pyridin-4-yl)-carbamic acid 4-chloro-phenyl ester
0.005 - 0.13
1-(2-chloro-1-oxidopyridin-4-yl)-3-phenylurea
0.0001 - 0.006
1-imidazo[1,2-a]pyridin-7-yl-3-phenylurea
0.027
2-amino-6-(3-methoxyanilino)purine
Arabidopsis thaliana
-
-
0.0039
2-chloro-6-(3-chloroanilino)purine
Arabidopsis thaliana
-
-
0.0075
2-chloro-6-(3-fluoroanilino)purine
Arabidopsis thaliana
-
-
0.00375
2-chloro-6-(3-hydroxyanilino)purine
Arabidopsis thaliana
-
-
0.061
2-chloro-6-(3-methoxyanilino)-9-methylpurine
Arabidopsis thaliana
-
-
0.0019
2-chloro-6-(3-methoxyanilino)purine
Arabidopsis thaliana
-
-
0.0254
2-chloro-6-(4-chloroanilino)purine
Arabidopsis thaliana
-
-
0.05
2-chloro-6-(4-fluoroanilino)purine
Arabidopsis thaliana
-
-
0.08
2-chloro-6-anilinopurine
Arabidopsis thaliana
-
-
0.001
2-fluoro-6-(3-methoxyanilino)purine
Arabidopsis thaliana
-
-
0.014
2-nitro-6-(3-methoxyanilino)purine
Arabidopsis thaliana
-
-
0.0124
6-(3-methoxyanilino)purine
Arabidopsis thaliana
-
-
0.005 - 0.05
N-(1,2,3-thidiazol-5-yl)-N'-phenylurea
0.002 - 0.009
N-(2,6-dichloro-pyridin-4-yl)-N'-benzylurea
0.005 - 0.02
N-(2,6-dichloro-pyridin-4-yl)-N'-phenoxyurea
0.00008 - 0.0045
N-(2,6-dichloro-pyridin-4-yl)-N'-phenylurea
0.0011 - 0.002
N-(2,6-dichloropyridin-4-yl)-N'-benzyl-N'-methylurea
0.006 - 0.032
N-(2-amino-6-chloro-pyridin-4-yl)-N'-benzylurea
0.00004 - 0.0018
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
0.00004 - 0.035
N-(2-amino-pyridin-4-yl)-N'-phenylurea
0.006 - 0.022
N-(2-chloro-6-methoxy-pyridin-4-yl)-N'-benzylurea
0.0015 - 0.018
N-(2-chloro-pyridin-4-yl)-N'-benzylurea
0.035 - 0.055
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
0.02 - 2
N6-but-2,3-dienyl-aminopurine
Solanum tuberosum
-
mechanism-based irreversible (suicide) inhibitor. IC50: 0.02 mM with N6-(2-isopentenyl)adenine as substrate, 0.0004 mM with N6-(2-isopentenyl)adenosine as substrate and less than 0.0001 mM with zeatin as substrate
0.029
thidiazuron
Arabidopsis thaliana
-
-
additional information
additional information
Arabidopsis thaliana
-
IC50-values above 0.1 mM for 2-chloro-6-(2-hydroxyanilino)purine, 2-chloro-6-(4-hydroxyanilino)purine, 2-chloro-6-(2-methoxyanilino)purine, 2-chloro-6-(4-methoxyanilino)purine, 2-methylthio-6-(3-methoxyanilino)purine and 2-chloro-6-(3-methoxyanilino)-9-isopropylpurine, no inhibition observed for 6-anilinopurine and trans-zeatin
-
0.004
(2,6-dichloro-pyridin-4-yl)-carbamic acid benzyl ester
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.007
(2,6-dichloro-pyridin-4-yl)-carbamic acid benzyl ester
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.007
(2,6-dichloro-pyridin-4-yl)-carbamic acid benzyl ester
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.009
(2,6-dichloro-pyridin-4-yl)-carbamic acid benzyl ester
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.0002
(2-chloro-pyridin-4-yl)-carbamic acid 4-chloro-phenyl ester
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.006
(2-chloro-pyridin-4-yl)-carbamic acid 4-chloro-phenyl ester
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.006
(2-chloro-pyridin-4-yl)-carbamic acid 4-chloro-phenyl ester
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.039
(2-chloro-pyridin-4-yl)-carbamic acid 4-chloro-phenyl ester
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.005
1-(2-chloro-1-oxidopyridin-4-yl)-3-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.015
1-(2-chloro-1-oxidopyridin-4-yl)-3-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.017
1-(2-chloro-1-oxidopyridin-4-yl)-3-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.13
1-(2-chloro-1-oxidopyridin-4-yl)-3-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.0001
1-imidazo[1,2-a]pyridin-7-yl-3-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.0004
1-imidazo[1,2-a]pyridin-7-yl-3-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.001
1-imidazo[1,2-a]pyridin-7-yl-3-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.006
1-imidazo[1,2-a]pyridin-7-yl-3-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.005
N-(1,2,3-thidiazol-5-yl)-N'-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.015
N-(1,2,3-thidiazol-5-yl)-N'-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.017
N-(1,2,3-thidiazol-5-yl)-N'-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.05
N-(1,2,3-thidiazol-5-yl)-N'-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.002
N-(2,6-dichloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.003
N-(2,6-dichloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.004
N-(2,6-dichloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.009
N-(2,6-dichloro-pyridin-4-yl)-N'-benzylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.005
N-(2,6-dichloro-pyridin-4-yl)-N'-phenoxyurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.005
N-(2,6-dichloro-pyridin-4-yl)-N'-phenoxyurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.008
N-(2,6-dichloro-pyridin-4-yl)-N'-phenoxyurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.02
N-(2,6-dichloro-pyridin-4-yl)-N'-phenoxyurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.00008
N-(2,6-dichloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.0004
N-(2,6-dichloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.0005
N-(2,6-dichloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.0045
N-(2,6-dichloro-pyridin-4-yl)-N'-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.0011
N-(2,6-dichloropyridin-4-yl)-N'-benzyl-N'-methylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.0015
N-(2,6-dichloropyridin-4-yl)-N'-benzyl-N'-methylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.002
N-(2,6-dichloropyridin-4-yl)-N'-benzyl-N'-methylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.002
N-(2,6-dichloropyridin-4-yl)-N'-benzyl-N'-methylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.006
N-(2-amino-6-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.022
N-(2-amino-6-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.024
N-(2-amino-6-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.032
N-(2-amino-6-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.00004
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.0006
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.0007
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.0018
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.00004
N-(2-amino-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.002
N-(2-amino-pyridin-4-yl)-N'-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.032
N-(2-amino-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.035
N-(2-amino-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.006
N-(2-chloro-6-methoxy-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.015
N-(2-chloro-6-methoxy-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.02
N-(2-chloro-6-methoxy-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.022
N-(2-chloro-6-methoxy-pyridin-4-yl)-N'-benzylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.0015
N-(2-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.003
N-(2-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.004
N-(2-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.018
N-(2-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.035
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.042
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.045
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.055
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
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40000 - 60000
-
gel filtration
47900
-
x * 47900, amino acid sequence calculation
49800
-
x * 49800, amino acid sequence calculation
53300
-
x * 61000, SDS-PAGE, weak bands also at 75000 Da and100000 Da, x * 53300, calculated from the deduced amino acid sequence
55000 - 94400
-
gel filtration
55700
x * 55700, about, sequence calculation
5600
1 * 5600, deglycosylated enzyme, SDS-PAGE
56000
-
x * 59100, OsCKX1, amino acid sequence calculation, x * 56000, OsCKX2, amino acid sequence calculation, x * 58000, OsCKX3and OsCKX5, amino acid sequence calculation, x * 58400, OsCKX4, amino acid sequence calculation
56500
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
57057
x * 60000, SDS-PAGE, x * 57057, mass spectrometry
57200
x * 57200, amino acid sequence calculation
57400
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
57900
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
57966
x * 57966, calculated from the deduced amino acid sequence
58000
-
x * 59100, OsCKX1, amino acid sequence calculation, x * 56000, OsCKX2, amino acid sequence calculation, x * 58000, OsCKX3and OsCKX5, amino acid sequence calculation, x * 58400, OsCKX4, amino acid sequence calculation
58080
x * 92000, SDS-PAGE, x * 59720, sequence calculation, x * 58080, mass spectrometry
58400
-
x * 59100, OsCKX1, amino acid sequence calculation, x * 56000, OsCKX2, amino acid sequence calculation, x * 58000, OsCKX3and OsCKX5, amino acid sequence calculation, x * 58400, OsCKX4, amino acid sequence calculation
59100
-
x * 59100, OsCKX1, amino acid sequence calculation, x * 56000, OsCKX2, amino acid sequence calculation, x * 58000, OsCKX3and OsCKX5, amino acid sequence calculation, x * 58400, OsCKX4, amino acid sequence calculation
59400
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
59720
x * 92000, SDS-PAGE, x * 59720, sequence calculation, x * 58080, mass spectrometry
59900
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
60383
x * 60383, calculated from the deduced amino acid sequence
60400
x * 60400, DsCKX1, amino acid sequence calculation
61000
-
x * 61000, SDS-PAGE, weak bands also at 75000 Da and100000 Da, x * 53300, calculated from the deduced amino acid sequence
63000
-
x * 69000, recombinant enzyme, SDS-PAGE, x * 63000, native enzyme, SDS-PAGE
64000
gel filtration, MALDI-MS
64290
x * 97000, SDS-PAGE, x * 65050, sequence calculation, x * 64290, mass spectrometry
64900
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
65050
x * 97000, SDS-PAGE, x * 65050, sequence calculation, x * 64290, mass spectrometry
69000
-
x * 69000, recombinant enzyme, SDS-PAGE, x * 63000, native enzyme, SDS-PAGE
69865
1 * 69865, MALDI-TOF MS, crystal structure analysis
92000
x * 92000, SDS-PAGE, x * 59720, sequence calculation, x * 58080, mass spectrometry
97000
x * 97000, SDS-PAGE, x * 65050, sequence calculation, x * 64290, mass spectrometry
58100
x * 58100, HvCKX3, amino acid sequence calculation
58100
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
58800
x * 58800, amino acid sequence calculation
58800
x * 58800, HvCKX2, amino acid sequence calculation
60000
-
non denaturing PAGE
60000
x * 60000, SDS-PAGE, x * 57057, mass spectrometry
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Galuszka, P.; Frebort, I.; Sebela, M.; Sauer, P.; Jacobsen, S.; Pec, P.
Cytokinin oxidase or dehydrogenase? Mechanism of cytokinin degradation in cereals
Eur. J. Biochem.
268
450-461
2001
Hordeum vulgare, Triticum aestivum
brenda
Burch, L.R.; Horgan, R.
The purification of cytokinin oxidase from Zea mays kernels
Phytochemistry
28
1313-1319
1989
Triticum aestivum, Zea mays
-
brenda
McGaw, B.A.; Horgan, R.
Cytokinin catabolism and cytokinin oxidase
Phytochemistry
22
1103-1105
1983
Zea mays
-
brenda
Motyka, V.; Faiss, M.; Strnad, M.; Kaminek, M.; Schmuelling, T.
Changes in cytokinin content and cytokinin oxidase activity in response to derepression of ipt gene transcription in transgenic tobacco calli and plants
Plant Physiol.
112
1035-1043
1996
Nicotiana tabacum
brenda
Chatfield, J.M.; Armstrong, D.J.
Cytokinin oxidase from Phaseolus vulgaris callus tissues. Enhanced in vitro activity of the enzyme in the presence of copper-imidazole complexes
Plant Physiol.
84
726-731
1987
Phaseolus vulgaris
brenda
Bilyeu, K.D.; Cole, J.L.; Laskey, J.G.; Riekhof, W.R.; Esparza, T.J.; Kramer, M.D.; Morris, R.O.
Molecular and biochemical characterization of a cytokinin oxidase from maize
Plant Physiol.
125
378-386
2001
Zea mays
brenda
Chatfield, J.M.; Armstrong, D.J.
Regulation of cytokinin oxidase activity in callus tissues of Phaseolus vulgaris L. cv Great Northern
Plant Physiol.
80
493-499
1986
Phaseolus vulgaris
brenda
Galuszka, P.; Frebort, I.; Sebela, M.; Pec, P.
Degradation of cytokinins by cytokinin oxidases in plants
Plant Growth Regul.
32
315-327
2000
Catharanthus roseus, Nicotiana tabacum, Phaseolus lunatus, Populus x canadensis, Triticum aestivum, Zea mays
-
brenda
Hare, P.D.; van Staden, J.
Cytokinin oxidase: biochemical features and physiological significance
Physiol. Plant.
91
128-136
1994
Catharanthus roseus, Glycine max, Nicotiana tabacum, Phaseolus lunatus, Phaseolus vulgaris, Populus x canadensis, Triticum aestivum, Zea mays
-
brenda
Dietrich, J.T.; Kaminek, M.; Blevins, D.G.; Reinbott, T.M.; Morris, R.O.
Changes in cytokinins and cytokinin oxidase activity in developing maize kernels and the effects of exogenous cytokinin on kernel development
Plant Physiol. Biochem.
33
327-336
1995
Zea mays
-
brenda
Auer, C.A.; Motyka, V.; Brezinova, A.; Kaminek, M.
Endogenous cytokinin accumulation and cytokinin oxidase activity during shoot organogenesis of Petunia hybrida
Physiol. Plant.
105
141-147
1999
Petunia x hybrida
-
brenda
Wang, J.; Letham, D.S.
Cytokinin oxidase - purification by affinity chromatography and activation by caffeic acid
Plant Sci.
112
161-166
1995
Nicotiana tabacum
-
brenda
Kopecny, D.; Briozzo, P.; Joly, N.; Houba-Herin, N.; Madzak, C.; Pethe, C.; Laloue, M.
Purification, crystallization and preliminary X-ray diffraction study of a recombinant cytokinin oxidase from Zea mays
Acta Crystallogr. Sect. D
60
1500-1501
2004
Zea mays
brenda
Frebortova, J.; Fraaije, M.W.; Galuszka, P.; Sebela, M.; Pec, P.; Hrbac, J.; Novak, O.; Bilyeu, K.D.; English, J.T.; Frebort, I.
Catalytic reaction of cytokinin dehydrogenase: preference for quinones as electron acceptors
Biochem. J.
380
121-130
2004
Zea mays (Q9T0N8), Zea mays
brenda
Galuszka, P.; Frebortova, J.; Werner, T.; Yamada, M.; Strnad, M.; Schmulling, T.; Frebort, I.
Cytokinin oxidase/dehydrogenase genes in barley and wheat: cloning and heterologous expression
Eur. J. Biochem.
271
3990-4002
2004
Hordeum vulgare, Hordeum vulgare (Q84U27), Hordeum vulgare (Q8H6F6), Hordeum vulgare (Q94KI4), Triticum aestivum (Q94KI5), Triticum aestivum
brenda
Malito, E.; Coda, A.; Bilyeu, K.D.; Fraaije, M.W.; Mattevi, A.
Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis
J. Mol. Biol.
341
1237-1249
2004
Zea mays (Q9T0N8), Zea mays
brenda
Schmulling, T.; Werner, T.; Riefler, M.; Krupkova, E.; Bartrina y Manns, I.
Structure and function of cytokinin oxidase/dehydrogenase genes of maize, rice, Arabidopsis and other species
J. Plant Res.
116
241-252
2003
Dictyostelium discoideum, Nicotiana tabacum, no activity in Saccharomyces cerevisiae, no activity in Pichia pastoris, no activity in Synechocystis sp., Nostoc sp., Oryza sativa, Phaseolus sp., no activity in Prochlorococcus marinus, no activity in Physcomitrella patens, no activity in Raphanus sativus, Rhodococcus fascians, Hordeum vulgare (Q8H6F6), Dendrobium hybrid cultivar (Q9FE45), Arabidopsis thaliana (Q9FUJ3), Arabidopsis thaliana, Zea mays (Q9T0N8), Zea mays, no activity in Synechocystis sp. PCC 6803
brenda
Motyka, V.; Vankova, R.; Capkova, V.; Petrasek, J.; Kaminek, M.; Schmulling, T.
Cytokinin-induced upregulation of cytokinin oxidase activity in tobacco includes changes in enzyme glycosylation and secretion
Physiol. Plant.
117
11-21
2003
Nicotiana tabacum
-
brenda
Galuszka, P.; Frebortova, J.; Luhova, L.; Bilyeu, K.D.; English, J.T.; Frebort, I.
Tissue localization of cytokinin dehydrogenase in maize: possible involvement of quinone species generated from plant phenolics by other enzymatic systems in the catalytic reaction
Plant Cell Physiol.
46
716-728
2005
Zea mays (Q9T0N8), Zea mays, Zea mays ZmCKX1 (Q9T0N8)
brenda
Laskey, J.G.; Patterson, P.; Bilyeu, K.; Morris, R.O.
Rate enhancement of cytokinin oxidase/dehydrogenase using 2,6-dichlorophenolindophenol as an electron acceptor
Plant Growth Regul.
40
189-196
2003
Zea mays
-
brenda
Vaseva-Gemisheva, I.; Lee, D.; Alexieva, V.; Karanov, E.
Cytokinin oxidase/dehydrogenase in Pisum sativum plants during vegetative development. Influence of UV-B irradiation and high temperature on enzymatic activity
Plant Growth Regul.
42
1-5
2004
Pisum sativum
-
brenda
Blagoeva, E.; Dobrev, P.I.; Malbeck, J.; Motyka, V.; Gaudinova, A.; Vankova, R.
Effect of exogenous cytokinins, auxins and adenine on cytokinin N-glucosylation and cytokinin oxidase/dehydrogenase activity in de-rooted radish seedlings
Plant Growth Regul.
44
15-23
2004
Raphanus sativus
-
brenda
Popelkova, H.; Fraaije, M.W.; Novak, O.; Frebortova, J.; Bilyeu, K.D.; Frebort, I.
Kinetic and chemical analyses of the cytokinin dehydrogenase-catalysed reaction: correlations with the crystal structure
Biochem. J.
398
113-124
2006
Zea mays
brenda
Kopecny, D.; Pethe, C.; Sebela, M.; Houba-Herin, N.; Madzak, C.; Majira, A.; Laloue, M.
High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica
Biochimie
87
1011-1022
2005
Zea mays (Q9T0N8), Zea mays
brenda
Novakova, M.; Motyka, V.; Dobrev, P.I.; Malbeck, J.; Gaudinova, A.; Vankova, R.
Diurnal variation of cytokinin, auxin and abscisic acid levels in tobacco leaves
J. Exp. Bot.
56
2877-2883
2005
Nicotiana tabacum
brenda
Gaudinova, A.; Dobrev, P.I.; Solcova, B.; Novak, O.; Strnad, M.; Friedecky, D.; Motyka, V.
The involvement of cytokinin oxidase/dehydrogenase and zeatin reductase in regulation of cytokinin levels in pea (Pisum sativum L.) leaves
J. Plant Growth Regul.
24
188-200
2005
Pisum sativum
-
brenda
Sriskandarajah, S.; Prinsen, E.; Motyka, V.; Dobrev, P.I.; Serek, M.
Regenerative capacity of cacti Schlumbergera and Rhipsalidopsis in relation to endogenous phytohormones, cytokinin oxidase/dehydrogenase, and peroxidase activities
J. Plant Growth Regul.
25
79-88
2006
Rhipsalidopsis sp., Schlumbergera sp.
-
brenda
Suttle, J.C.; Mornet, R.
Mechanism-based irreversible inhibitors of cytokinin dehydrogenase
J. Plant Physiol.
162
1189-1196
2005
Solanum tuberosum
brenda
Ashikari, M.; Sakakibara, H.; Lin, S.; Yamamoto, T.; Takashi, T.; Nishimura, A.; Angeles, E.R.; Qian, Q.; Kitano, H.; Matsuoka, M.
Cytokinin oxidase regulates rice grain production
Science
309
741-745
2005
Oryza sativa
brenda
Ananieva, K.I.; Stirk, W.A.; Kaminek, M.; van Staden, J.
Some biochemical properties of cytokinin oxidase/dehydrogenase in Cucurbita pepo L. (zucchini) leaves
South Afr. J. Bot.
71
253-256
2005
Cucurbita pepo
-
brenda
Valdes, A.E.; Galuszka, P.; Fernandez, B.; Centeno, M.L.; Frebort, I.
Developmental stage as a possible factor affecting cytokinin content and cytokinin dehydrogenase activity in Pinus sylvestris
Biol. Plant.
51
193-197
2007
Pinus sylvestris
-
brenda
Todorova, D.; Vaseva, I.; Malbeck, J.; Travnickova, A.; Machackova, I.; Karanov, E.
Cytokinin oxidase/dehydrogenase activity as a tool in gibberellic acid/cytokinin cross talk
Biol. Plant.
51
579-583
2007
Pisum sativum (A0MQ40)
-
brenda
Frebortova, J.; Galuszka, P.; Werner, T.; Schmulling, T.; Frebort, I.
Functional expression and purification of cytokinin dehydrogenase from Arabidopsis thaliana (AtCKX2) in Saccharomyces cerevisiae
Biol. Plant.
51
673-682
2007
Arabidopsis thaliana
-
brenda
Carabelli, M.; Possenti, M.; Sessa, G.; Ciolfi, A.; Sassi, M.; Morelli, G.; Ruberti, I.
Canopy shade causes a rapid and transient arrest in leaf development through auxin-induced cytokinin oxidase activity
Genes Dev.
21
1863-1868
2007
Arabidopsis thaliana
brenda
Kopecny, D.; Sebela, M.; Briozzo, P.; Spichal, L.; Houba-Herin, N.; Masek, V.; Joly, N.; Madzak, C.; Anzenbacher, P.; Laloue, M.
Mechanism-based inhibitors of cytokinin oxidase/dehydrogenase attack FAD cofactor
J. Mol. Biol.
380
886-899
2008
Zea mays (Q9T0N8), Zea mays
brenda
Held, M.; Pepper, A.N.; Bozdarov, J.; Smith, M.D.; Emery, R.J.; Guinel, F.C.
The pea nodulation mutant R50 (sym16) displays altered activity and expression profiles for cytokinin dehydrogenase
J. Plant Growth Regul.
27
170-180
2008
Pisum sativum (A0MQ40)
-
brenda
Conrad, K.; Motyka, V.; Schlueter, T.
Increase in activity, glycosylation and expression of cytokinin oxidase/dehydrogenase during the senescence of barley leaf segments in the dark
Physiol. Plant.
130
572-579
2007
Hordeum vulgare
brenda
von Schwartzenberg, K.; Nunez, M.F.; Blaschke, H.; Dobrev, P.I.; Novak, O.; Motyka, V.; Strnad, M.
Cytokinins in the bryophyte Physcomitrella patens: Analyses of activity, distribution, and cytokinin oxidase/dehydrogenase overexpression reveal the role of extracellular cytokinins
Plant Physiol.
145
786-800
2007
Physcomitrium patens, Arabidopsis thaliana (Q9FUJ3)
brenda
Bae, E.; Bingman, C.A.; Bitto, E.; Aceti, D.J.; Phillips, G.N.
Crystal structure of Arabidopsis thaliana cytokinin dehydrogenase
Proteins
70
303-306
2007
Arabidopsis thaliana (Q9FUJ1), Arabidopsis thaliana
brenda
Zatloukal, M.; Gemrotova, M.; Dolezal, K.; Havlicek, L.; Spichal, L.; Strnad, M.
Novel potent inhibitors of A. thaliana cytokinin oxidase/dehydrogenase
Bioorg. Med. Chem.
16
9268-9275
2008
Arabidopsis thaliana
brenda
Smehilova, M.; Galuszka, P.; Bilyeu, K.D.; Jaworek, P.; Kowalska, M.; Sebela, M.; Sedlarova, M.; English, J.T.; Frebort, I.
Subcellular localization and biochemical comparison of cytosolic and secreted cytokinin dehydrogenase enzymes from maize
J. Exp. Bot.
60
2701-2712
2009
Zea mays (B6V8F7), Zea mays (Q9T0N8), Zea mays
brenda
Wang, Y.; Luo, J.P.; Wei, Z.J.; Zhang, J.C.
Molecular cloning and expression analysis of a cytokinin oxidase (DhCKX) gene in Dendrobium huoshanense
Mol. Biol. Rep.
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2008
Dendrobium huoshanense (A2TLJ3), Dendrobium huoshanense
brenda
Ananieva, K.; Ananiev, E.D.; Doncheva, S.; Georgieva, K.; Tzvetkova, N.; Kaminek, M.; Motyka, V.; Dobrev, P.; Gajdosova, S.; Malbeck, J.
Senescence progression in a single darkened cotyledon depends on the light status of the other cotyledon in Cucurbita pepo (zucchini) seedlings: potential involvement of cytokinins and cytokinin oxidase/dehydrogenase activity
Physiol. Plant.
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2008
Cucurbita pepo
brenda
Kopecny, D.; Briozzo, P.; Popelkova, H.; Sebela, M.; Koncitikova, R.; Spichal, L.; Nisler, J.; Madzak, C.; Frebort, I.; Laloue, M.; Houba-Herin, N.
Phenyl- and benzylurea cytokinins as competitive inhibitors of cytokinin oxidase/dehydrogenase: a structural study
Biochimie
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1052-1062
2010
Zea mays (Q9T0N8), Zea mays
brenda
Zalewski, W.; Galuszka, P.; Gasparis, S.; Orczyk, W.; Nadolska-Orczyk, A.
Silencing of the HvCKX1 gene decreases the cytokinin oxidase/dehydrogenase level in barley and leads to higher plant productivity
J. Exp. Bot.
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1839-1851
2010
Triticum aestivum, Hordeum vulgare (Q94KI4), Hordeum vulgare
brenda
Schlueter, T.; Leide, J.; Conrad, K.
Light promotes an increase of cytokinin oxidase/dehydrogenase activity during senescence of barley leaf segments
J. Plant Physiol.
168
694-698
2011
Hordeum vulgare, Zea mays, Phragmites australis
brenda
Frebortova, J.; Novak, O.; Frebort, I.; Jorda, R.
Degradation of cytokinins by maize cytokinin dehydrogenase is mediated by free radicals generated by enzymatic oxidation of natural benzoxazinones
Plant J.
61
467-481
2010
Zea mays
brenda
Saravanakumar, A.; Aslam, A.; Shajahan, A.
Histochemical localization of cytokinin oxidase/dehydrogenase during the developmental stages of Withania somnifera (L.) Dunal
Afr. J. Biotechnol.
10
8800-8804
2011
Withania somnifera
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brenda
Avalbaev, A.M.; Somov, K.A.; Yuldashev, R.A.; Shakirova, F.M.
Cytokinin oxidase is key enzyme of cytokinin degradation
Biochemistry (Moscow)
77
1354-1361
2012
Arabidopsis thaliana, Hordeum vulgare, Nicotiana tabacum, Oryza sativa, Physcomitrium patens, Populus sp., Zea mays, Selaginella moellendorffii
brenda
Cueno, M.E.; Imai, K.; Ochiai, K.; Okamoto, T.
Cytokinin dehydrogenase differentially regulates cytokinin and indirectly affects hydrogen peroxide accumulation in tomato leaf
J. Plant Physiol.
169
834-838
2012
Solanum lycopersicum, Solanum lycopersicum Improved Pope
brenda
Kowalska, M.; Galuszka, P.; Frebortova, J.; Sebela, M.; Beres, T.; Hluska, T.; Smehilova, M.; Bilyeu, K.D.; Frebort, I.
Vacuolar and cytosolic cytokinin dehydrogenases of Arabidopsis thaliana: heterologous expression, purification and properties
Phytochemistry
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1970-1978
2010
Arabidopsis thaliana, Arabidopsis thaliana (O22213), Arabidopsis thaliana (Q9LTS3)
brenda
Ma, X.; Feng, D.; Wang, H.; Li, X.; Kong, L.
Cloning and expression analysis of wheat cytokinin oxidase/dehydrogenase gene TaCKX3
Plant Mol. Biol. Rep.
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98-105
2011
Triticum aestivum (D3JAJ5), Triticum aestivum Yanyou 361 (D3JAJ5)
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brenda
Yuldashev, R.; Avalbaev, A.; Bezrukova, M.; Vysotskaya, L.; Khripach, V.; Shakirova, F.
Cytokinin oxidase is involved in the regulation of cytokinin content by 24-epibrassinolide in wheat seedlings
Plant Physiol. Biochem.
55
1-6
2012
Triticum aestivum, Triticum aestivum Bashkirskaya 24
brenda
Vysotskaya, L.; Avalbaev, A.; Yuldashev, R.; Shakirova, F.; Veselov, S.; Kudoyarova, G.
Regulation of cytokinin oxidase activity as a factor affecting the content of cytokinins
Russ. J. Plant Physiol.
57
494-500
2010
Triticum turgidum subsp. durum, Triticum turgidum subsp. durum Bezenchukskaya 139
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brenda
Marques, M.; Freitas, B.; Guedes, T.; Fernandes, R.
Cytokinin dehydrogenase activity in primary roots and characterization of primary metabolites from leaves and rootlets of Ricinus communis
Braz. Arch. Biol. Technol.
56
904-910
2013
Ricinus communis
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brenda
Ma, Y.; Zheng, L.; Xie, R.; He, S.; Deng, L.
Genome-wide identification and analysis of CKX genes in Poncirus trifoliata
J. Hortic. Sci. Biotechnol.
91
592-602
2016
Citrus trifoliata
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brenda
Pospisilova, H.; Jiskrova, E.; Vojta, P.; Mrizova, K.; Kokas, F.; Cudejkova, M.M.; Bergougnoux, V.; Plihal, O.; Klimesova, J.; Novak, O.; Dzurova, L.; Frebort, I.; Galuszka, P.
Transgenic barley overexpressing a cytokinin dehydrogenase gene shows greater tolerance to drought stress
New Biotechnol.
33
692-705
2016
Arabidopsis thaliana (O22213), Arabidopsis thaliana
brenda
Zalabak, D.; Johnova, P.; Plihal, O.; Senkova, K.; Samajova, O.; Jiskrova, E.; Novak, O.; Jackson, D.; Mohanty, A.; Galuszka, P.
Maize cytokinin dehydrogenase isozymes are localized predominantly to the vacuoles
Plant Physiol. Biochem.
104
114-124
2016
Zea mays, Zea mays (B6V8F7), Zea mays (E3T1X0), Zea mays (E3T1X1), Zea mays (E3T1X2), Zea mays (E3T1X3), Zea mays (Q9T0N8)
brenda
Zalabak, D.; Galuszka, P.; Mrizova, K.; Podle?akova, K.; Gu, R.; Frebortova, J.
Biochemical characterization of the maize cytokinin dehydrogenase family and cytokinin profiling in developing maize plantlets in relation to the expression of cytokinin dehydrogenase genes
Plant Physiol. Biochem.
74
283-293
2014
Zea mays, Zea mays (E3T1X1), Zea mays (Q9T0N8)
brenda
Frebortova, J.; Greplova, M.; Seidl, M.F.; Heyl, A.; Frebort, I.
Biochemical characterization of putative adenylate dimethylallyltransferase and cytokinin dehydrogenase from Nostoc sp. PCC 7120
PLoS ONE
10
e0138468
2015
no activity in Nostoc sp. PCC 7120
brenda
Mrizova, K.; Jiskrova, E.; Vyroubalova, S.; Novak, O.; Ohnoutkova, L.; Pospisilova, H.; Frebort, I.; Harwood, W.A.; Galuszka, P.
Overexpression of cytokinin dehydrogenase genes in barley (Hordeum vulgare cv. Golden Promise) fundamentally affects morphology and fertility
PLoS ONE
8
e79029
2013
Hordeum vulgare (I3VIX5), Hordeum vulgare
brenda
Tian, F.; Greplova, M.; Frebort, I.; Dale, N.; Napier, R.
A highly selective biosensor with nanomolar sensitivity based on cytokinin dehydrogenase
PLoS ONE
9
e90877
2014
Zea mays (Q9T0N8), Zea mays
brenda
Tsago, Y.; Chen, Z.; Cao, H.; Sunusi, M.; Khan, A.; Shi, C.; Jin, X.
Rice gene, OsCKX2-2, regulates inflorescence and grain size by increasing endogenous cytokinin content
Plant Growth Regul.
92
283-294
2020
Oryza sativa Japonica Group (Q4ADV8)
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brenda
Czajkowska, B.; Finlay, C.; Jones, G.; Brown, T.
Diversity of a cytokinin dehydrogenase gene in wild and cultivated barley
PLoS ONE
14
e0225899
2019
Hordeum vulgare
brenda
Yu, K.; Yu, Y.; Bian, L.; Ni, P.; Ji, X.; Guo, D.; Zhang, G.; Yang, Y.
Genome-wide identification of cytokinin oxidases/dehydrogenase (CKXs) in grape and expression during berry set
Sci. Hortic.
280
109917
2021
Vitis vinifera (D7TS26), Vitis vinifera (D7TSA7), Vitis vinifera (D7U3H6), Vitis vinifera (F6H1K3), Vitis vinifera (F6H3S4), Vitis vinifera (F6HGV7), Vitis vinifera (F6HHY5), Vitis vinifera (F6HZZ3)
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brenda