Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
(1R)-1-(4-chlorophenyl)ethan-1-amine + H2O + O2
1-(4-chlorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(1R)-1-phenylethan-1-amine + H2O + O2
1-phenylacetaldehyde + NH3 + H2O2
-
-
-
-
?
(1R,2R)-2-aminocyclohexanol + O2 + H2O
cyclohexanone + NH3 + H2O2
the enzyme shows highly R-selective deamination activity toward beta-amino alcohols
-
-
?
(1R,2R)-2-aminocyclopentanol + O2 + H2O
cyclopentanone + NH3 + H2O2
the enzyme shows highly R-selective deamination activity toward beta-amino alcohols
-
-
?
(1R,2S)-1-amino-2-indanol + O2 + H2O
? + NH3 + H2O2
the enzyme shows highly R-selective deamination activity toward beta-amino alcohols
-
-
?
(1S)-1-(4-chlorophenyl)ethan-1-amine + H2O + O2
1-(4-chlorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(1S)-1-phenylethan-1-amine + H2O + O2
1-phenylacetaldehyde + NH3 + H2O2
-
-
-
-
?
(1S)-1-phenylpropan-1-amine + H2O + O2
1-phenylpropan-1-one + NH3 + H2O2
-
-
-
-
?
(1S,2R)-1-amino-2-indanol + O2 + H2O
? + NH3 + H2O2
the enzyme shows highly R-selective deamination activity toward beta-amino alcohols
-
-
?
(1S,2S)-2-aminocyclohexanol + O2 + H2O
cyclohexanone + NH3 + H2O2
the enzyme shows highly R-selective deamination activity toward beta-amino alcohols
-
-
?
(1S,2S)-2-aminocyclopentanol + O2 + H2O
cyclopentanone + NH3 + H2O2
the enzyme shows highly R-selective deamination activity toward beta-amino alcohols
-
-
?
(2R)-heptan-2-amine + H2O + O2
heptan-2-one + NH3 + H2O2
-
-
-
-
?
(2S)-heptan-2-amine + H2O + O2
heptan-2-one + NH3 + H2O2
-
-
-
-
?
(R)-1-(4-chlorophenyl)ethylamine + O2 + H2O
1-(4-chlorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(R)-1-(4-fluorophenyl)ethanamine + O2 + H2O
1-(4-fluorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(R)-1-aminotetraline + O2 + H2O
?
-
-
-
-
?
(R)-2-heptylamine + O2 + H2O
heptan-2-one + NH3 + H2O2
(S)-1-(4-chlorophenyl)ethylamine + O2 + H2O
1-(4-chlorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(S)-1-(4-fluorophenyl)ethanamine + O2 + H2O
1-(4-fluorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(S)-1-aminoindan + O2 + H2O
?
-
-
-
-
?
(S)-1-aminotetraline + O2 + H2O
?
-
-
-
-
?
(S)-1-aminotetraline + O2 + H2O
tetralone + NH3 + H2O2
-
-
-
-
?
(S)-1-p-tolylethanamine + O2 + H2O
1-(4-methylphenyl)ethanone + NH3 + H2O2
-
-
-
-
?
(S)-1-phenylethanamine + O2 + H2O
? + NH3 + H2O2
(S)-1-phenylethylamine + O2 + H2O
?
-
-
-
-
?
(S)-1-phenylpropan-1-amine + O2 + H2O
1-phenylpropionaldehyde + NH3 + H2O2
-
-
-
-
?
(S)-2-aminohexane + O2 + H2O
hexan-2-one + NH3 + H2O2
-
-
-
-
?
(S)-2-heptylamine + O2 + H2O
heptan-2-one + NH3 + H2O2
-
25% activity compared to cyclohexylamine
-
-
?
(S)-alpha-methylbenzylamine + O2 + H2O
?
-
55% activity compared to cyclohexylamine
-
-
?
(S)-N-benzyl-1-phenylethylamine + O2 + H2O
?
-
-
-
-
?
1,2,3,4-tetrahydro-2-naphthylamine + O2 + H2O
? + NH3 + H2O2
-
23% of the activity compared to cyclohexylamine
-
?
1,2-cyclohexanediamine + O2 + H2O
cyclohexaneamine + NH3 + H2O2
-
18% of the activity compared to cyclohexylamine
-
?
1-(4-chlorophenyl)ethanamine + O2 + H2O
?
-
35% activity compared to cyclohexylamine
-
-
?
1-(4-fluorophenyl)ethanamine + O2 + H2O
1-(4-fluorophenyl)ethanone + NH3 + H2O2
-
-
-
-
?
1-(4-fluorophenyl)ethanamine + O2 + H2O
?
-
61% activity compared to cyclohexylamine
-
-
?
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline + + O2 + H2O
?
1-(4-methylphenyl)ethanamine + O2 + H2O
?
-
5% activity compared to cyclohexylamine
-
-
?
1-(4-methylphenyl)methanamine + O2 + H2O
?
-
1% activity compared to cyclohexylamine
-
-
?
1-(naphthalen-1-yl)ethanamine + O2 + H2O
?
-
1% activity compared to cyclohexylamine
-
-
?
1-indanamine + O2 + H2O
1-indanone + NH3 + H2O2
-
27% activity compared to cyclohexylamine
-
-
?
1-phenylethanamine + O2 + H2O
1-phenylacetaldehyde + NH3 + H2O2
-
-
-
-
?
1-phenylethanamine + O2 + H2O
1-phenylethanone + NH3 + H2O2
-
48% activity compared to cyclohexylamine
-
-
?
2-amino-4-phenylbutane + O2 + H2O
4-phenylbutan-2-one + NH3 + H2O2
-
-
-
-
?
2-amino-5-methylhexane + O2 + H2O
5-methylhexane-2-one + NH3 + H2O2
-
-
-
-
?
2-aminocyclohexanol + O2 + H2O
?
-
-
-
-
?
2-aminoheptane + O2 + H2O
heptan-2-one + NH3 + H2O2
-
-
-
-
?
2-aminonorbornane + O2 + H2O
?
-
-
-
-
?
2-aminopentane + O2 + H2O
pentan-2-one + NH3 + H2O2
-
-
-
-
?
2-ethyl-1-hexylamine + O2 + H2O
2-ethylhexanaldehyde + NH3 + H2O2
-
-
-
-
?
2-heptylamine + O2 + H2O
heptan-2-one + NH3 + H2O2
-
24% activity compared to cyclohexylamine
-
-
?
2-methyl-1,2,3,4-tetrahydroquinoline + O2 + H2O
(R)-2-methyl-1,2,3,4-tetrahydroquinoline + NH3 + H2O2
2-methylcyclohexanamine + O2 + H2O
2-methylcyclohexanone + NH3 + H2O2
2-methylcyclohexanamine + O2 + H2O
?
-
56% activity compared to cyclohexylamine
-
-
?
2-methylpropan-1-amine + O2 + H2O
?
-
0.1% activity compared to cyclohexylamine
-
-
?
3-phenylpropan-1-amine + H2O + O2
? + NH3 + H2O2
4-methylbenzylamine + O2 + H2O
4-methylbenzaldehyde + NH3 + H2O2
-
-
-
-
?
4-methylcyclohexanamine + O2 + H2O
4-methylcyclohexanone + NH3 + H2O2
-
41% of the activity with cyclohexylamine
-
-
?
4-methylcyclohexylamine + O2 + H2O
?
-
133% activity compared to cyclohexylamine
-
-
?
4-methylpiperidine + O2 + H2O
?
-
0.1% activity compared to cyclohexylamine
-
-
?
4-phenylbutan-2-amine + O2 + H2O
?
-
12% activity compared to cyclohexylamine
-
-
?
5-methylhexan-2-amine + O2 + H2O
?
-
9% activity compared to cyclohexylamine
-
-
?
6-amino-2-methylheptan-2-ol + O2 + H2O
?
-
0.1% activity compared to cyclohexylamine
-
-
?
benzylamine + O2 + H2O
benzaldehyde + NH3 + H2O2
bicyclo[2.2.1]heptan-2-amine + O2 + H2O
?
-
2% activity compared to cyclohexylamine
-
-
?
butan-2-amine + O2 + H2O
?
-
3% activity compared to cyclohexylamine
-
-
?
cycloheptanamine + O2 + H2O
?
-
75% activity compared to cyclohexylamine
-
-
?
cycloheptylamine + O2 + H2O
cycloheptanone + NH3 + H2O2
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
cyclooctanamine + O2 + H2O
?
-
23% activity compared to cyclohexylamine
-
-
?
cyclooctanamine + O2 + H2O
cyclooctanone + NH3 + H2O2
-
-
-
-
?
cyclopentylamine + O2 + H2O
cyclopentanone + NH3 + H2O2
hexan-1-amine + O2 + H2O
?
-
1% activity compared to cyclohexylamine
-
-
?
L-valine ethyl ester
D-valine ethyl ester
N-methylcyclohexanamine + O2 + H2O
?
N-methylcyclohexylamine + O2 + H2O
cyclohexanone + methylamine + H2O2
racemic phenylalanine ethyl ester
L-phenylalanine ethyl ester
racemic valine ethyl ester
D-valine ethyl ester
secondary butylamine + O2 + H2O
butanone + NH3 + H2O2
trans-2-aminocyclohexanol + O2 + H2O
?
-
16% activity compared to cyclohexylamine
-
-
?
additional information
?
-
(R)-2-heptylamine + O2 + H2O
heptan-2-one + NH3 + H2O2
-
0.1% activity compared to cyclohexylamine
-
-
?
(R)-2-heptylamine + O2 + H2O
heptan-2-one + NH3 + H2O2
-
0.1% activity compared to cyclohexylamine
-
-
?
(S)-1-phenylethanamine + O2 + H2O
? + NH3 + H2O2
-
-
-
-
?
(S)-1-phenylethanamine + O2 + H2O
? + NH3 + H2O2
-
-
-
-
?
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline + + O2 + H2O
?
-
the enzyme is able to completely deracemize 100 mM 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline under Turner's deracemization conditions to afford (S)-1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline in 80% isolated yield and 99% nantiomeric excess at a semipreparative scale (0.4 mmol)
-
-
?
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline + + O2 + H2O
?
-
the enzyme is able to completely deracemize 100 mM 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline under Turner's deracemization conditions to afford (S)-1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline in 80% isolated yield and 99% nantiomeric excess at a semipreparative scale (0.4 mmol)
-
-
?
2-methyl-1,2,3,4-tetrahydroquinoline + O2 + H2O
(R)-2-methyl-1,2,3,4-tetrahydroquinoline + NH3 + H2O2
-
-
-
-
?
2-methyl-1,2,3,4-tetrahydroquinoline + O2 + H2O
(R)-2-methyl-1,2,3,4-tetrahydroquinoline + NH3 + H2O2
-
-
-
-
?
2-methylcyclohexanamine + O2 + H2O
2-methylcyclohexanone + NH3 + H2O2
-
22% of the activity with cyclohexylamine
-
-
?
2-methylcyclohexanamine + O2 + H2O
2-methylcyclohexanone + NH3 + H2O2
-
-
-
-
?
3-phenylpropan-1-amine + H2O + O2
? + NH3 + H2O2
-
7% activity compared to cyclohexylamine
-
-
?
3-phenylpropan-1-amine + H2O + O2
? + NH3 + H2O2
-
7% activity compared to cyclohexylamine
-
-
?
benzylamine + O2 + H2O
benzaldehyde + NH3 + H2O2
-
-
-
-
?
benzylamine + O2 + H2O
benzaldehyde + NH3 + H2O2
-
-
-
-
?
cycloheptylamine + O2 + H2O
cycloheptanone + NH3 + H2O2
-
55% of the activity with cyclohexylamine
-
-
?
cycloheptylamine + O2 + H2O
cycloheptanone + NH3 + H2O2
-
42% of the activity compared to cyclohexylamine
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
best substrate
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
100% activity
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
best substrate
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
100% activity
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
-
-
-
?
cyclohexylamine + O2 + H2O
cyclohexanone + NH3 + H2O2
-
highly specific for alicyclic primary amines, oxygen is the only electron acceptor
-
?
cyclopentylamine + O2 + H2O
cyclopentanone + NH3 + H2O2
-
7% of the activity with cyclohexylamine
-
-
?
cyclopentylamine + O2 + H2O
cyclopentanone + NH3 + H2O2
-
best substrate
-
-
?
cyclopentylamine + O2 + H2O
cyclopentanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
cyclopentylamine + O2 + H2O
cyclopentanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
L-valine ethyl ester
D-valine ethyl ester
-
isomerization reaction
-
-
?
L-valine ethyl ester
D-valine ethyl ester
-
isomerization reaction
-
-
?
N-methylcyclohexanamine + O2 + H2O
?
-
-
-
-
?
N-methylcyclohexanamine + O2 + H2O
?
-
6% activity compared to cyclohexylamine
-
-
?
N-methylcyclohexylamine + O2 + H2O
cyclohexanone + methylamine + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
N-methylcyclohexylamine + O2 + H2O
cyclohexanone + methylamine + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
racemic phenylalanine ethyl ester
L-phenylalanine ethyl ester
-
deracemization reaction
-
-
?
racemic phenylalanine ethyl ester
L-phenylalanine ethyl ester
-
deracemization reaction
-
-
?
racemic valine ethyl ester
D-valine ethyl ester
-
deracemization reaction
-
-
?
racemic valine ethyl ester
D-valine ethyl ester
-
deracemization reaction
-
-
?
secondary butylamine + O2 + H2O
butanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
secondary butylamine + O2 + H2O
butanone + NH3 + H2O2
-
highly specific for alicyclic monoamines and aliphatic monoamines
-
?
additional information
?
-
-
deracemization of 1-aminotetraline by coupling wild type enzyme with a nonselective reducing agent NH3·BH3 is a route to norsertraline
-
-
?
additional information
?
-
-
no activity with (R)-alpha-methylbenzylamine, 2-methylpiperidine and tetrahydroquinaldine
-
-
?
additional information
?
-
-
trace activity with (R)-2-aminohexane, 1-hexylamine, (R)-(-)-1-phenylethylamine, (R)-1-p-tolylethanamine, (R)-1-aminoindan, (S)-(-)-Nalpha-dimethylbenzylamine, 2-methylpiperidine, 4-methylpiperidine, 2-methyl-1,2,3,4-tetrahydroquinoline, and N,N-dimethylcyclohexylamine. No activity with 1-naphthalen-1-ylethanamine
-
-
?
additional information
?
-
-
when cyclohexylamine oxidase in combination with a borane-ammonia complex as reducing agent is applied to the deracemization of several substrates, excellent enantiomeric ratios (higher than 99:1) and good isolated yields (62-75%) of the corresponding (R)-amines are obtained
-
-
?
additional information
?
-
-
no activitiy towards (R)-N-(prop-2-yn-1-yl)-2, 3-dihydro-1H-inden-1-amine, 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, (S)-N-methyl-1-phenylethanamine, and 1-methyl-1,2,3,4-tetrahydroisoquinoline
-
-
?
additional information
?
-
-
deracemization of 1-aminotetraline by coupling wild type enzyme with a nonselective reducing agent NH3·BH3 is a route to norsertraline
-
-
?
additional information
?
-
-
trace activity with (R)-2-aminohexane, 1-hexylamine, (R)-(-)-1-phenylethylamine, (R)-1-p-tolylethanamine, (R)-1-aminoindan, (S)-(-)-Nalpha-dimethylbenzylamine, 2-methylpiperidine, 4-methylpiperidine, 2-methyl-1,2,3,4-tetrahydroquinoline, and N,N-dimethylcyclohexylamine. No activity with 1-naphthalen-1-ylethanamine
-
-
?
additional information
?
-
-
no activity with (R)-alpha-methylbenzylamine, 2-methylpiperidine and tetrahydroquinaldine
-
-
?
additional information
?
-
-
when cyclohexylamine oxidase in combination with a borane-ammonia complex as reducing agent is applied to the deracemization of several substrates, excellent enantiomeric ratios (higher than 99:1) and good isolated yields (62-75%) of the corresponding (R)-amines are obtained
-
-
?
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.
1.3
(1R,2R)-2-aminocyclohexanol
pH 7.0, 30°C
-
1.1
(1R,2R)-2-aminocyclopentanol
pH 7.0, 30°C
-
0.6
(1R,2S)-1-amino-2-indanol
pH 7.0, 30°C
-
0.7
(1S,2R)-1-amino-2-indanol
pH 7.0, 30°C
-
1
(1S,2S)-2-aminocyclohexanol
pH 7.0, 30°C
-
0.9
(1S,2S)-2-aminocyclopentanol
pH 7.0, 30°C
-
0.07 - 0.32
(S)-1-aminotetraline
0.56 - 1.03
(S)-1-phenylethanamine
0.36 - 6.54
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
0.27 - 1.12
2-methyl-1,2,3,4-tetrahydroquinoline
0.25 - 7.71
Cyclohexylamine
0.22 - 2.04
cyclooctanamine
1.1 - 7.5
L-valine ethyl ester
-
0.07
(S)-1-aminotetraline
-
mutant enzyme Y321F, at pH 6.5 and 30°C
0.08
(S)-1-aminotetraline
-
mutant enzyme Y321A, at pH 6.5 and 30°C
0.08
(S)-1-aminotetraline
-
wild type enzyme, at pH 6.5 and 30°C
0.21
(S)-1-aminotetraline
-
mutant enzyme L353M, at pH 6.5 and 30°C
0.26
(S)-1-aminotetraline
-
mutant enzyme M226A, at pH 6.5 and 30°C
0.32
(S)-1-aminotetraline
-
mutant enzyme L199A, at pH 6.5 and 30°C
0.56
(S)-1-phenylethanamine
-
wild type enzyme, at pH 6.5 and 30°C
0.66
(S)-1-phenylethanamine
-
mutant enzyme M226F, at pH 6.5 and 30°C
0.79
(S)-1-phenylethanamine
-
mutant enzyme Y459T, at pH 6.5 and 30°C
0.91
(S)-1-phenylethanamine
-
mutant enzyme L199T, at pH 6.5 and 30°C
0.99
(S)-1-phenylethanamine
-
mutant enzyme T198F, at pH 6.5 and 30°C
0.99
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
1.03
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
0.36
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme P396A
-
0.52
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme F327A
-
0.53
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme G202A
-
0.61
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme L200A
-
1.24
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme T203A
-
1.84
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme I201A
-
1.88
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme L295I
-
2.13
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme F317A
-
2.2
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, wild-type enzyme
-
2.71
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme I173A
-
6.54
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme L295A
-
0.27
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
0.29
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme Y459T, at pH 6.5 and 30°C
0.36
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
0.62
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme M226F, at pH 6.5 and 30°C
0.69
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F, at pH 6.5 and 30°C
1.06
2-methyl-1,2,3,4-tetrahydroquinoline
-
wild type enzyme, at pH 6.5 and 30°C
1.12
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme L199T, at pH 6.5 and 30°C
0.25
Cyclohexylamine
-
-
0.25
Cyclohexylamine
-
pH 7.0, 30°C
0.25
Cyclohexylamine
-
pH 7.0, 50°C
1.08
Cyclohexylamine
-
wild type enzyme, at pH 6.5 and 30°C
2.28
Cyclohexylamine
-
mutant enzyme Y321F, at pH 6.5 and 30°C
3.39
Cyclohexylamine
-
mutant enzyme L353M, at pH 6.5 and 30°C
4.76
Cyclohexylamine
-
mutant enzyme M226A, at pH 6.5 and 30°C
5.94
Cyclohexylamine
-
mutant enzyme Y321A, at pH 6.5 and 30°C
7.71
Cyclohexylamine
-
mutant enzyme L199A, at pH 6.5 and 30°C
0.22
cyclooctanamine
-
mutant enzyme Y321F, at pH 6.5 and 30°C
0.24
cyclooctanamine
-
mutant enzyme Y321A, at pH 6.5 and 30°C
0.59
cyclooctanamine
-
wild type enzyme, at pH 6.5 and 30°C
1.89
cyclooctanamine
-
mutant enzyme M226A, at pH 6.5 and 30°C
1.91
cyclooctanamine
-
mutant enzyme L199A, at pH 6.5 and 30°C
2.04
cyclooctanamine
-
mutant enzyme L353M, at pH 6.5 and 30°C
1.1
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I
-
1.2
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/ M226T
-
1.8
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/T198I
-
2.7
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/M226T/T198I
-
5
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme T198I
-
5.1
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme M226T
-
5.2
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme L199F
-
5.8
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/M226T/T198I/F199F
-
7.5
L-valine ethyl ester
-
pH and temperature not specified in the publication, wild-type enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5.8
(1R,2R)-2-aminocyclohexanol
pH 7.0, 30°C
-
5.6
(1R,2R)-2-aminocyclopentanol
pH 7.0, 30°C
-
4.9
(1R,2S)-1-amino-2-indanol
pH 7.0, 30°C
-
1.2
(1S,2R)-1-amino-2-indanol
pH 7.0, 30°C
-
1.5
(1S,2S)-2-aminocyclohexanol
pH 7.0, 30°C
-
1.6
(1S,2S)-2-aminocyclopentanol
pH 7.0, 30°C
-
2.96 - 10.62
(S)-1-aminotetraline
0.16 - 4.15
(S)-1-phenylethanamine
0.027 - 0.26
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
0.003 - 0.31
2-methyl-1,2,3,4-tetrahydroquinoline
4.77 - 523
Cyclohexylamine
3.03 - 7.68
cyclooctanamine
0.55 - 3.69
L-valine ethyl ester
-
2.96
(S)-1-aminotetraline
-
mutant enzyme Y321A, at pH 6.5 and 30°C
3.32
(S)-1-aminotetraline
-
mutant enzyme Y321F, at pH 6.5 and 30°C
5.72
(S)-1-aminotetraline
-
wild type enzyme, at pH 6.5 and 30°C
7.14
(S)-1-aminotetraline
-
mutant enzyme L199A, at pH 6.5 and 30°C
8.54
(S)-1-aminotetraline
-
mutant enzyme M226A, at pH 6.5 and 30°C
10.62
(S)-1-aminotetraline
-
mutant enzyme L353M, at pH 6.5 and 30°C
0.16
(S)-1-phenylethanamine
-
mutant enzyme Y459T, at pH 6.5 and 30°C
0.19
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
0.29
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
0.76
(S)-1-phenylethanamine
-
mutant enzyme L199T, at pH 6.5 and 30°C
1.4
(S)-1-phenylethanamine
-
mutant enzyme T198F, at pH 6.5 and 30°C
1.55
(S)-1-phenylethanamine
-
mutant enzyme M226F, at pH 6.5 and 30°C
4.15
(S)-1-phenylethanamine
-
wild type enzyme, at pH 6.5 and 30°C
0.027
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme I201A
-
0.039
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme F317A
-
0.048
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme T203A
-
0.056
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme L200A
-
0.057
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme F327A
-
0.084
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme L295I
-
0.097
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme G202A
-
0.111
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme I173A
-
0.12
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme L295A
-
0.135
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, wild-type enzyme
-
0.26
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme P396A
-
0.003
2-methyl-1,2,3,4-tetrahydroquinoline
-
wild type enzyme, at pH 6.5 and 30°C
0.06
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme M226F, at pH 6.5 and 30°C
0.15
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F, at pH 6.5 and 30°C
0.23
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme L199T, at pH 6.5 and 30°C
0.25
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
0.27
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme Y459T, at pH 6.5 and 30°C
0.31
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
4.77
Cyclohexylamine
-
mutant enzyme L199A, at pH 6.5 and 30°C
8.52
Cyclohexylamine
-
mutant enzyme Y321A, at pH 6.5 and 30°C
10.93
Cyclohexylamine
-
mutant enzyme Y321F, at pH 6.5 and 30°C
11.48
Cyclohexylamine
-
wild type enzyme, at pH 6.5 and 30°C
15.25
Cyclohexylamine
-
mutant enzyme L353M, at pH 6.5 and 30°C
16.33
Cyclohexylamine
-
mutant enzyme M226A, at pH 6.5 and 30°C
432
Cyclohexylamine
-
pH 7.0, 30°C
523
Cyclohexylamine
-
pH 7.0, 50°C
3.03
cyclooctanamine
-
wild type enzyme, at pH 6.5 and 30°C
3.44
cyclooctanamine
-
mutant enzyme Y321A, at pH 6.5 and 30°C
3.79
cyclooctanamine
-
mutant enzyme Y321F, at pH 6.5 and 30°C
6.62
cyclooctanamine
-
mutant enzyme L199A, at pH 6.5 and 30°C
7.06
cyclooctanamine
-
mutant enzyme M226A, at pH 6.5 and 30°C
7.68
cyclooctanamine
-
mutant enzyme L353M, at pH 6.5 and 30°C
0.55
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme M226T
-
0.64
L-valine ethyl ester
-
pH and temperature not specified in the publication, wild-type enzyme
-
0.92
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme L199F
-
1.09
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme T198I
-
1.25
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I
-
2.18
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/T198I
-
3.1
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/ M226T
-
3.54
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/M226T/T198I
-
3.69
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/M226T/T198I/F199F
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.5
(1R,2R)-2-aminocyclohexanol
pH 7.0, 30°C
-
5.1
(1R,2R)-2-aminocyclopentanol
pH 7.0, 30°C
-
8.2
(1R,2S)-1-amino-2-indanol
pH 7.0, 30°C
-
1.7
(1S,2R)-1-amino-2-indanol
pH 7.0, 30°C
-
1.5
(1S,2S)-2-aminocyclohexanol
pH 7.0, 30°C
-
1.8
(1S,2S)-2-aminocyclopentanol
pH 7.0, 30°C
-
22.31 - 71.5
(S)-1-aminotetraline
0.19 - 7.42
(S)-1-phenylethanamine
0.0147 - 0.722
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
0.003 - 1.15
2-methyl-1,2,3,4-tetrahydroquinoline
0.62 - 2075
Cyclohexylamine
3.47 - 17.23
cyclooctanamine
0.085 - 2.54
L-valine ethyl ester
-
22.31
(S)-1-aminotetraline
-
mutant enzyme L199A, at pH 6.5 and 30°C
32.85
(S)-1-aminotetraline
-
mutant enzyme M226A, at pH 6.5 and 30°C
37
(S)-1-aminotetraline
-
mutant enzyme Y321A, at pH 6.5 and 30°C
47.43
(S)-1-aminotetraline
-
mutant enzyme Y321F, at pH 6.5 and 30°C
50.57
(S)-1-aminotetraline
-
mutant enzyme L353M, at pH 6.5 and 30°C
71.5
(S)-1-aminotetraline
-
wild type enzyme, at pH 6.5 and 30°C
0.19
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
0.21
(S)-1-phenylethanamine
-
mutant enzyme Y459T, at pH 6.5 and 30°C
0.28
(S)-1-phenylethanamine
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
0.84
(S)-1-phenylethanamine
-
mutant enzyme L199T, at pH 6.5 and 30°C
1.42
(S)-1-phenylethanamine
-
mutant enzyme T198F, at pH 6.5 and 30°C
2.35
(S)-1-phenylethanamine
-
mutant enzyme M226F, at pH 6.5 and 30°C
7.42
(S)-1-phenylethanamine
-
wild type enzyme, at pH 6.5 and 30°C
0.0147
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme I201A
-
0.0183
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme F317A
-
0.0183
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme L295A
-
0.0387
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme T203A
-
0.04
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme I173A
-
0.0446
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme L295I
-
0.06135
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, wild-type enzyme
-
0.0918
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme L200A
-
0.1096
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme F327A
-
0.183
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme G202A
-
0.722
1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
-
pH 7.5, 45°C, mutant enzyme P396A
-
0.003
2-methyl-1,2,3,4-tetrahydroquinoline
-
wild type enzyme, at pH 6.5 and 30°C
0.1
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme M226F, at pH 6.5 and 30°C
0.2
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme L199T, at pH 6.5 and 30°C
0.22
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F, at pH 6.5 and 30°C
0.68
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S, at pH 6.5 and 30°C
0.92
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme Y459T, at pH 6.5 and 30°C
1.15
2-methyl-1,2,3,4-tetrahydroquinoline
-
mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C
0.62
Cyclohexylamine
-
mutant enzyme L199A, at pH 6.5 and 30°C
1.43
Cyclohexylamine
-
mutant enzyme Y321A, at pH 6.5 and 30°C
3.43
Cyclohexylamine
-
mutant enzyme M226A, at pH 6.5 and 30°C
4.49
Cyclohexylamine
-
mutant enzyme L353M, at pH 6.5 and 30°C
4.79
Cyclohexylamine
-
mutant enzyme Y321F, at pH 6.5 and 30°C
10.63
Cyclohexylamine
-
wild type enzyme, at pH 6.5 and 30°C
1724
Cyclohexylamine
-
pH 7.0, 30°C
2075
Cyclohexylamine
-
pH 7.0, 50°C
3.47
cyclooctanamine
-
mutant enzyme L199A, at pH 6.5 and 30°C
3.74
cyclooctanamine
-
mutant enzyme M226A, at pH 6.5 and 30°C
3.76
cyclooctanamine
-
mutant enzyme L353M, at pH 6.5 and 30°C
5.14
cyclooctanamine
-
wild type enzyme, at pH 6.5 and 30°C
14.33
cyclooctanamine
-
mutant enzyme Y321A, at pH 6.5 and 30°C
17.23
cyclooctanamine
-
mutant enzyme Y321F, at pH 6.5 and 30°C
0.085
L-valine ethyl ester
-
pH and temperature not specified in the publication, wild-type enzyme
-
0.108
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme M226T
-
0.18
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme L199F
-
0.22
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme T198I
-
0.64
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/M226T/T198I/F199F
-
1.1
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I
-
1.2
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/T198I
-
1.3
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/M226T/T198I
-
2.54
L-valine ethyl ester
-
pH and temperature not specified in the publication, mutant enzyme Y321I/ M226T
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.002
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme W63A
0.006
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme L295Y
0.007
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme L174A
0.009
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme Y433A
0.011
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme Q208A
0.013
-
with 2-ethyl-1-hexylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.015
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme F342A
0.016
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme W325A
0.018
-
with (R)-1-(4-chlorophenyl)ethylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.053
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme I201A
0.074
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme F317A
0.08
-
with N-methylcyclohexanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.084
-
with (R)-1-(4-fluorophenyl)ethanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.089
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme T203A
0.09
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme F327A
0.11
-
with 4-methylbenzylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.116
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme L200A
0.152
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme L295A
0.166
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme L295I
0.177
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme G202A
0.194
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme I173A
0.26
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, wild-type enzyme
0.27
-
with (S)-1-p-tolylethanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.33
-
with cyclopentylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.34
-
with benzylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
0.461
-
substrate: 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, pH 7.5, 45°C, mutant enzyme P396A
0.68
-
with 2-amino-4-phenylbutane as substrate, wild type enzyme, at pH 6.5 and 30°C
0.97
-
with 2-aminocyclohexanol as substrate, wild type enzyme, at pH 6.5 and 30°C
1.033
-
with cyclooctanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
1.13
-
with 2-aminopentane as substrate, wild type enzyme, at pH 6.5 and 30°C
1.2
-
with 2-aminoheptane as substrate, wild type enzyme, at pH 6.5 and 30°C
1.49
-
with 2-aminonorbornane hydrochloride as substrate, wild type enzyme, at pH 6.5 and 30°C
1.66
-
with (S)-1-phenylpropropan-1-amine as substrate, wild type enzyme, at pH 6.5 and 30°C
2.35
-
with (S)-1-aminoindan as substrate, wild type enzyme, at pH 6.5 and 30°C
2.36
-
with 1-phenylethanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
2.62
-
with (S)-1-(4-chlorophenyl)ethylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
2.79
-
with (S)-2-aminohexane as substrate, wild type enzyme, at pH 6.5 and 30°C
3.058
-
with 2-methylcyclohexanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
3.37
-
with 1-(4-fluorophenyl)ethanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
3.51
-
with (S)-(-)-1-phenylethylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
3.6
-
with 2-amino-5-methylhexane as substrate, wild type enzyme, at pH 6.5 and 30°C
4.56
-
with (S)-1-(4-fluorophenyl)ethanamine as substrate, wild type enzyme, at pH 6.5 and 30°C
5.6
-
with cyclohexylamine as substrate, wild type enzyme, at pH 6.5 and 30°C
5.69
-
with (S)-1-aminotetraline as substrate, wild type enzyme, at pH 6.5 and 30°C
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.
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.
F317A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 30% of the wild-type value
F327A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 179% of the wild-type value
G202A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 298% of the wild-type value
I173A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 67% of the wild-type value
I201A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 24% of the wild-type value
L200A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 150% of the wild-type value
L295A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 30% of the wild-type value
L295I
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 73% of the wild-type value
P396A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 1177% of the wild-type value
T203A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 63% of the wild-type value
F317A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 30% of the wild-type value
-
G202A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 298% of the wild-type value
-
I201A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 24% of the wild-type value
-
L200A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 150% of the wild-type value
-
T203A
-
kcat/Km for 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline is 63% of the wild-type value
-
L199A
-
the mutant shows generally lower activity (decrease of 15-97%) towards most substrates compared to wild type enzyme with the exception of the larger substrates, such as cyclooctanamine and bicyclic (S)-1-aminotetraline
L199I
-
the mutant is more active than the wild type enzyme toward the primary amines
L353M
-
the mutant shows 7-445% higher activity towards primary aliphatic amines with cycloalkane or aromatic moieties
M226F
-
the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
M226I
-
the mutant is more active than the wild type enzyme toward the primary amines
T198A
-
the mutant exhibits enhanced activity relative to the wild type enzyme for most (S)-enantiomers of primary amines and some secondary amines
T198F/L199S
-
the mutant exhibits 240times higher catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline than the wild type enzyme. The mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine compared to the wild type enzyme
Y321I/ M226T
-
29.8fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme. Chemoenzymatic deracemization is applied to prepare D-valine from racemic valine ethyl ester or L-valine ethyl ester in high yield (up to 95%) with excellent optical purity (more than 99% enantiomeric excess) by employing cyclohexylamine oxidase (CHAO) variant Y321I/M226T exhibiting catalytic efficiency that is 30 times higher than that of the wild type enzyme
Y321I/ M226T/L199F
-
mutant failed to be expressed
Y321I/L199F
-
mutant failed to be expressed
Y321I/M226T
-
the double mutant acts on (S)-N-(prop-2-yn-1-yl)-2,3-dihydro-1H-inden-1-amine
Y321I/M226T/T198I
-
15.1fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
Y321I/M226T/T198I/F199F
-
7.5fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
Y321I/T198I
-
14.2fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
Y321T
-
the mutation enhances the enzyme activity toward the secondary amines
Y459T
-
the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
L199A
-
the mutant shows generally lower activity (decrease of 15-97%) towards most substrates compared to wild type enzyme with the exception of the larger substrates, such as cyclooctanamine and bicyclic (S)-1-aminotetraline
-
L199F
-
2.1fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
-
L199T
-
the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
-
L353M
-
the mutant shows 7-445% higher activity towards primary aliphatic amines with cycloalkane or aromatic moieties
-
M226A
-
the mutant displays an enhanced activity (5-400%) towards most substrates
-
M226F
-
the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
-
M226T
-
1.3fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
-
T198F
-
the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
-
T198F/L199S
-
the mutant exhibits 240times higher catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline than the wild type enzyme. The mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine compared to the wild type enzyme
-
T198F/L199S/M226F
-
the mutant exhibits 406times higher catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline than the wild type enzyme. The mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine compared to the wild type enzyme
-
T198I
-
2.55fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
-
Y321A
-
the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
-
Y321F
-
the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
-
Y321I
-
13fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
-
Y321I/T198I
-
14.2fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
-
L199F
-
the mutant is more active than the wild type enzyme toward the primary amines
L199F
-
2.1fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
L199T
-
the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
L199T
-
the mutation enhances the enzyme activity toward the secondary amines
M226A
-
the mutant displays an enhanced activity (5-400%) towards most substrates
M226A
-
the mutant exhibits enhanced activity relative to the wild type enzyme for most (S)-enantiomers of primary amines and some secondary amines
M226T
-
the mutant is more active than the wild type enzyme toward the primary amines
M226T
-
1.3fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
T198F
-
the mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine and increased catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline compared to the wild type enzyme
T198F
-
the mutation enhances the enzyme activity toward the secondary amines
T198F/L199S/M226F
-
the mutant exhibits 406times higher catalytic efficiency with 2-methyl-1,2,3,4-tetrahydroquinoline than the wild type enzyme. The mutant shows reduced catalytic efficiency with (S)-1-phenylethanamine compared to the wild type enzyme
T198F/L199S/M226F
-
the substrate 2-methyl-1, 2, 3, 4-tetrahydroquinoline is deracemized by the triple mutant
T198I
-
the mutant is more active than the wild type enzyme toward the primary amines
T198I
-
2.55fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
Y321A
-
the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
Y321A
-
the mutation enhances the enzyme activity toward the secondary amines
Y321F
-
the mutant shows higher catalytic efficiency towards cyclooctanamine compared to the wild type enzyme
Y321F
-
the mutation enhances the enzyme activity toward the secondary amines
Y321I
-
the mutation enhances the enzyme activity toward the secondary amines and displays an enhanced catalytic efficiency toward 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline
Y321I
-
13fold increase of kcat/Km for the substrate L-valine ethyl ester as compared to wild-type enzyme
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.
Tokieda, T.; Niimura, T.; Takamura,F.; Yamaha, T.
Purification and some properties of cyclohexylamine oxidase from a Pseudomonas sp.
J. Biochem.
81
851-858
1977
Pseudomonas sp.
brenda
Iwaki, H.; Shimizu, M.; Tokuyama, T.; Hasegawa, Y.
Biodegradation of cyclohexylamine by Brevibacterium oxydans IH-35A
Appl. Environ. Microbiol.
65
2232-2234
1999
Microbacterium oxydans, Microbacterium oxydans IH-35A
brenda
Iwaki, H.; Shimizu, M.; Tokuyama, T.; Hasegawa, Y.
Purification and characterization of a novel cyclohexylamine oxidase from the cyclohexylamine-degrading Brevibacterium oxydans IH-35A
J. Biosci. Bioeng.
88
264-268
1999
Microbacterium oxydans, Microbacterium oxydans IH-35A
brenda
Li, G.; Ren, J.; Iwaki, H.; Zhang, D.; Hasegawa, Y.; Wu, Q.; Feng, J.; Lau, P.C.; Zhu, D.
Substrate profiling of cyclohexylamine oxidase and its mutants reveals new biocatalytic potential in deracemization of racemic amines
Appl. Microbiol. Biotechnol.
98
1681-1689
2014
Microbacterium oxydans, Microbacterium oxydans IH-35A
brenda
Leisch, H.; Grosse, S.; Iwaki, H.; Hasegawa, Y.; Lau, P.
Cyclohexylamine oxidase as a useful biocatalyst for the kinetic resolution and dereacemization of amines
Can. J. Chem.
90
39-45
2012
Microbacterium oxydans, Microbacterium oxydans IH-35A
-
brenda
Mirza, I.A.; Burk, D.L.; Xiong, B.; Iwaki, H.; Hasegawa, Y.; Grosse, S.; Lau, P.C.; Berghuis, A.M.
Structural analysis of a novel cyclohexylamine oxidase from Brevibacterium oxydans IH-35A
PLoS ONE
8
e60072
2013
Microbacterium oxydans (M5AWH1), Microbacterium oxydans, Microbacterium oxydans IH-35A (M5AWH1)
brenda
Li, G.; Ren, J.; Yao, P.; Duan, Y.; Zhang, H.; Wu, Q.; Feng, J.; Lau, P.; Zhu, D.
Deracemization of 2-methyl-1,2,3,4-tetrahydroquinoline using mutant cyclohexylamine oxidase obtained by iterative saturation mutagenesis
ACS Catal.
4
903-908
2014
Microbacterium oxydans, Microbacterium oxydans IH-35A
-
brenda
Yan, D.Z.; Li, X.; Li, C.Z.; Mao, L.Q.; Chi, X.Q.; Zhou, N.Y.; Liu, D.Y.
Genome-wide identification and characterization of genes encoding cyclohexylamine degradation in a novel cyclohexylamine-degrading bacterial strain of Pseudomonas plecoglossicida NyZ12
J. Biotechnol.
251
166-173
2017
Pseudomonas plecoglossicida, Pseudomonas plecoglossicida NyZ12
brenda
Li, G.; Yao, P.; Cong, P.; Ren, J.; Wang, L.; Feng, J.; Lau, P.C.; Wu, Q.; Zhu, D.
New recombinant cyclohexylamine oxidase variants for deracemization of secondary amines by orthogonally assaying designed mutants with structurally diverse substrates
Sci. Rep.
6
24973
2016
Microbacterium oxydans
brenda
Zhang, J.D.; Chang, Y.W.; Dong, R.; Yang, X.X.; Gao, L.L.; Li, J.; Huang, S.P.; Guo, X.M.; Zhang, C.F.; Chang, H.H.
Enantioselective cascade biocatalysis for deracemization of racemic beta-amino alcohols to enantiopure (S)-beta-amino alcohols by employing cyclohexylamine oxidase and omega-transaminase
ChemBioChem
22
124-128
2021
Arthrobacter sp. TYUT010-15 (A0A7G7Y0T8)
brenda
Gong, R.; Yao, P.; Chen, X.; Feng, J.; Wu, Q.; Lau, P.; Zhu, D.
Accessing D-valine synthesis by improved variants of bacterial cyclohexylamine oxidase
ChemCatChem
10
387-390
2018
Microbacterium oxydans, Microbacterium oxydans IH-35A
-
brenda
Zhou, H.; Han, Z.G.; Fang, T.; Chen, Y.Y.; Ning, S.B.; Gan, Y.T.; Yan, D.Z.
Characterization of a new cyclohexylamine oxidase from Acinetobacter sp. YT-02
Front. Microbiol.
9
2848
2018
Acinetobacter sp. YT-02
brenda
Wu, X.; Huang, Z.; Wang, Z.; Li, Z.; Wang, J.; Lin, J.; Chen, F.
Asymmetric synthesis of a key dextromethorphan intermediate and its analogues enabled by a new cyclohexylamine oxidase Enzyme Discov. React. Dev. Mechanistic Insight
J. Org. Chem.
85
5598-5614
2020
Erythrobacteraceae bacterium, Erythrobacteraceae bacterium CCH12-C2
brenda