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1,3-propandiol + NAD+
? + NADH + H+
butanol + NAD+
butanal + NADH + H+
-
-
-
-
?
butanol + NAD+
butyraldehyde + NADH + H+
ethanol + NAD+
acetaldehyde + NADH + H+
ethanol + NAD+
ethanal + NADH
formaldehyde + NADH + H+
methanol + NAD+
isopropanol + NAD+
isopropanal + NADH + H+
-
low activity
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
methanol + NADP+
formaldehyde + NADPH + H+
n-butanol + NAD+
butyraldehyde + NADH + H+
n-butanol + NAD+
n-butanal + NADH
n-propanol + NAD+
n-propanal + NADH
n-propanol + NAD+
propionaldehyde + NADH + H+
propanol + NAD+
propanal + NADH + H+
-
-
-
-
?
propanol + NAD+
propionaldehyde + NADH + H+
additional information
?
-
1,3-propandiol + NAD+
? + NADH + H+
-
very low activity
-
-
?
1,3-propandiol + NAD+
? + NADH + H+
-
low activity
-
-
?
butanol + NAD+
butyraldehyde + NADH + H+
-
-
-
-
?
butanol + NAD+
butyraldehyde + NADH + H+
-
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
-
-
-
-
?
ethanol + NAD+
ethanal + NADH
-
-
-
-
?
ethanol + NAD+
ethanal + NADH
-
best substrate
-
-
?
ethanol + NAD+
ethanal + NADH
-
best substrate
-
-
r
formaldehyde + NADH + H+
methanol + NAD+
-
-
-
r
formaldehyde + NADH + H+
methanol + NAD+
-
Mdhs generally show higher activity and affinity for formaldehyde compared to methanol
-
-
r
formaldehyde + NADH + H+
methanol + NAD+
key step for both toxic formaldehyde elimination
-
-
r
formaldehyde + NADH + H+
methanol + NAD+
-
-
-
r
formaldehyde + NADH + H+
methanol + NAD+
key step for both toxic formaldehyde elimination
-
-
r
formaldehyde + NADH + H+
methanol + NAD+
-
Mdhs generally show higher activity and affinity for formaldehyde compared to methanol
-
-
r
formaldehyde + NADH + H+
methanol + NAD+
-
Mdhs generally show higher activity and affinity for formaldehyde compared to methanol
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
33% of activity with ethanol
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
44% of activity with ethanol, NADP+ cannot replace NAD+
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
no activity with 2-propanol, 2,3-butandiol, mannitol and glycerol
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
involved in initial methanol oxidation
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
involved in initial methanol oxidation
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
involved in initial methanol oxidation
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
involved in initial methanol oxidation
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
very low activity, Mdhs generally show higher activity and affinity for formaldehyde compared to methanol
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
very low activity. Mdhs generally show higher activity and affinity for formaldehyde compared to methanol
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
in nature, methanol dehydrogenase (Mdh), which converts methanol to formaldehyde, highly favors the reverse reaction
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
key step for ethanol production in bacterial methylotrophy
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
key step for ethanol production in bacterial methylotrophy
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
very low activity, Mdhs generally show higher activity and affinity for formaldehyde compared to methanol
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
very low activity. Mdhs generally show higher activity and affinity for formaldehyde compared to methanol
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
in nature, methanol dehydrogenase (Mdh), which converts methanol to formaldehyde, highly favors the reverse reaction
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
very low activity, Mdhs generally show higher activity and affinity for formaldehyde compared to methanol
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
very low activity. Mdhs generally show higher activity and affinity for formaldehyde compared to methanol
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
XoxF may not be involved in methylotrophy
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
-
-
-
-
r
methanol + NADP+
formaldehyde + NADPH + H+
Mdh enzyme mutant D41G, no activity of the wild-type enzyme with NADP(H)
-
-
r
methanol + NADP+
formaldehyde + NADPH + H+
Mdh enzyme mutant D98G, no activity of the wild-type enzyme with NADP(H)
-
-
r
methanol + NADP+
formaldehyde + NADPH + H+
Mdh enzyme mutant D98G, no activity of the wild-type enzyme with NADP(H)
-
-
r
methanol + NADP+
formaldehyde + NADPH + H+
Mdh enzyme mutant D41G, no activity of the wild-type enzyme with NADP(H)
-
-
r
n-butanol + NAD+
butyraldehyde + NADH + H+
-
-
-
r
n-butanol + NAD+
butyraldehyde + NADH + H+
-
-
-
r
n-butanol + NAD+
butyraldehyde + NADH + H+
-
-
-
r
n-butanol + NAD+
butyraldehyde + NADH + H+
-
-
-
r
n-butanol + NAD+
n-butanal + NADH
-
87% of activity with ethanol
-
?
n-butanol + NAD+
n-butanal + NADH
-
87% of activity with ethanol
-
r
n-propanol + NAD+
n-propanal + NADH
-
71% of activity with ethanol
-
?
n-propanol + NAD+
n-propanal + NADH
-
71% of activity with ethanol
-
r
n-propanol + NAD+
propionaldehyde + NADH + H+
-
-
-
r
n-propanol + NAD+
propionaldehyde + NADH + H+
-
-
-
-
?
n-propanol + NAD+
propionaldehyde + NADH + H+
-
-
-
-
?
propanol + NAD+
propionaldehyde + NADH + H+
-
-
-
r
propanol + NAD+
propionaldehyde + NADH + H+
-
-
-
r
additional information
?
-
-
all Mdh isozymes catalyze the oxidation of methanol, but the catalytic activity for methanol is considerably lower than for most other alcohols tested. The isozymes exhibit a broad and different substrate specificity range, and display both dehydrogenase and reductase activities. Isozyme Mdh3 shows the highest activity of all isozymes
-
-
?
additional information
?
-
efficient coupling with the irreversible sequestration of formaldehyde by 3-hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloseisomerase (Phi) serves as the key driving force to pull the pathway equilibrium toward central metabolism
-
-
?
additional information
?
-
I3DTM5
poor activity with 2-propanol and 1,2-popanediol
-
-
?
additional information
?
-
poor activity with 2-propanol and 1,2-popanediol
-
-
?
additional information
?
-
-
poor activity with 2-propanol and 1,2-popanediol
-
-
?
additional information
?
-
-
all Mdh isozymes catalyze the oxidation of methanol, but the catalytic activity for methanol is considerably lower than for most other alcohols tested. The isozymes exhibit a broad and different substrate specificity range, and display both dehydrogenase and reductase activities. Isozyme Mdh3 shows the highest activity of all isozymes
-
-
?
additional information
?
-
I3DTM5
poor activity with 2-propanol and 1,2-popanediol
-
-
?
additional information
?
-
poor activity with 2-propanol and 1,2-popanediol
-
-
?
additional information
?
-
efficient coupling with the irreversible sequestration of formaldehyde by 3-hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloseisomerase (Phi) serves as the key driving force to pull the pathway equilibrium toward central metabolism
-
-
?
additional information
?
-
-
all Mdh isozymes catalyze the oxidation of methanol, but the catalytic activity for methanol is considerably lower than for most other alcohols tested. The isozymes exhibit a broad and different substrate specificity range, and display both dehydrogenase and reductase activities. Isozyme Mdh3 shows the highest activity of all isozymes
-
-
?
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Act protein
activator protein, UniProt ID I3EA59, the in vitro activity of Lysinibacillus sphaericus Mdh is increased by the endogenous activator protein Act, a Nudix hydrolase
-
NudBC
a Nudix hydrolase from Bacillus coagulans, UniProt ID G2TKZ3
-
NudDK
a Nudix hydrolase from Desulfotomaculum kuznetsovii, UniProt ID F6CJI1
-
NudF protein
-
can be catalytically stimulated by the Bacillus subtilis NudF protein in vitro
-
NudLF
a Nudix hydrolase from Lysinibacillus fusiformis, UniProt ID D7WXY3
-
NudLS
a Nudix hydrolase from Lysinibacillus sphaericus, UniProt ID B1HRL7
-
Act
activator protein, UniProt ID I3EA59, the in vitro activity of Bacillus methanolicus Mdh is increased by the endogenous activator protein Act, a Nudix hydrolase, in a pH-dependent manner. Act increases the Vmax of the enzyme and decreases the Km for methanol, the increase was 23fold at pH 7.4 and 50fold at pH 9.0
-
Act
activator protein, UniProt ID I3EA59, the in vitro activity of Bacillus methanolicus Mdh is increased by the endogenous activator protein Act, a Nudix hydrolase, no activation in vivo
-
Act
activator protein, UniProt ID I3EA59, the in vitro activity of Bacillus methanolicus Mdh3 is increased by the endogenous activator protein Act, a Nudix hydrolase
-
Act
-
activator protein, UniProt ID I3EA59, the in vitro activity of Desulfitobacterium hafniense Adh is increased by the endogenous activator protein Act, a Nudix hydrolase
-
Act
-
activator protein, UniProt ID I3EA59, the in vitro activity of Bacillus coagulans Adh is increased by the endogenous activator protein Act, a Nudix hydrolase
-
Activator protein
-
-
-
Activator protein
-
activation in presence of Mg2+, in vitro: 3 mol soluble activator protein per mol enzyme, in vivo estimated as 1 mol per 17.5 mol enzyme, MW 50000 with two subunits of MW 27000 each, in presence of activator protein and Mg2+ enzyme possesses a high affinity active site for alcohol and NAD+, up to 40fold increase of activity, primarily of Vmax, slight decrease of Km-value for methanol, enzyme/activator-interaction is dilution-sensitive, no stimulation of formaldehyde reduction
-
Activator protein
-
each activator protein subunit binds one molecule of NADH, activator may facilitate oxidation of reduced enzyme bound NADH cofactor
-
activator protein ACT
-
all three isozymes are activated by ACT, which is encoded by gene act, overview
-
activator protein ACT
UniProt ID I3EA59, the in vitro activity of Bacillus methanolicus Mdh is increased by the endogenous activator protein Act, a Nudix hydrolase, in a pH-dependent manner. Act increases the Vmax of the enzyme and decreases the Km for methanol, the increase is 20fold at pH 7.4 and 9fold at pH 9.0
-
additional information
-
strongly stimulated by the ACT protein
-
additional information
-
strongly stimulated by the ACT protein
-
additional information
I3DTM5
the enzyme is activated by several Nudix hydrolases, relative activities of Adh enzymes, overview
-
additional information
the enzyme is activated by several Nudix hydrolases, relative activities of Adh enzymes, overview
-
additional information
-
the enzyme is activated by several Nudix hydrolases, relative activities of Adh enzymes, overview
-
additional information
Mdh2 from Cupriavidus necator does not require activation by and is insensitive to known activators such as Bacillus methanolicus ACT and Escherichia coli Nudix hydrolase NudF, or putative native Cupriavidus necator activators in the Nudix family under mesophilic condition. The enzyme exhibits higher or comparable activity and affinity toward methanol relative to the Bacillus methanolicus Mdh with or without activator ACT in a wide range of temperatures
-
additional information
-
Mdh2 from Cupriavidus necator does not require activation by and is insensitive to known activators such as Bacillus methanolicus ACT and Escherichia coli Nudix hydrolase NudF, or putative native Cupriavidus necator activators in the Nudix family under mesophilic condition. The enzyme exhibits higher or comparable activity and affinity toward methanol relative to the Bacillus methanolicus Mdh with or without activator ACT in a wide range of temperatures
-
additional information
-
no activation by activator protein Act, UniProt ID I3EA59
-
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0.5
butanol
-
pH 9.5, 55°C, wild-type enzyme
additional information
additional information
-
0.25
ethanol
-
pH 9.5, 55°C, wild-type enzyme
1.19
ethanol
-
pH 9.5, 55°C, mutant enzyme A164F
1.38
ethanol
-
pH 9.5, 55°C, mutant enzyme T141S
17.38
ethanol
-
pH 9.5, 55°C, mutant enzyme S101V
51
ethanol
recombinant enzyme, pH 7.4, 30°C, in presence of activator Act
161
ethanol
recombinant enzyme, pH 9.0, 30°C, in presence of activator Act
224
ethanol
recombinant enzyme, pH 9.0, 30°C, in absence of activator Act
225
ethanol
recombinant enzyme, pH 7.4, 30°C, in absence of activator Act
1
formaldehyde
-
pH 6.7, 45°C, isozyme Mdh3
1.1
formaldehyde
-
pH 6.7, 45°C, isozyme Mdh1
3
formaldehyde
-
pH 6.7, 45°C, isozyme Mdh1
4.5
formaldehyde
-
pH 6.7, 45°C, isozyme Mdh2
7
formaldehyde
-
pH 6.7, 45°C, isozyme Mdh2
7.1
formaldehyde
-
pH 6.7, 45°C, isozyme Mdh3
0.01
methanol
-
pH 9.5, 55°C, mutant enzyme E396V
0.0216
methanol
pH 9.5, 30°C, recombinant mutant A26V/A31V/A169V
0.0269
methanol
pH 9.5, 30°C, recombinant mutant A169V
0.0307
methanol
pH 9.5, 30°C, recombinant mutant A26V/A169V
0.046
methanol
-
pH 9.5, 55°C, mutant enzyme K318N
0.129
methanol
pH 9.5, 30°C, recombinant mutant A31V
0.132
methanol
pH 9.5, 30°C, recombinant wild-type enzyme
0.233
methanol
-
pH 9.5, 55°C, mutant enzyme E396V/K318N
0.372
methanol
-
pH 9.5, 55°C, mutant enzyme K46E
1.311
methanol
-
pH 9.5, 55°C, wild-type enzyme
3.23
methanol
-
pH 9.5, 55°C, wild-type enzyme
9
methanol
recombinant enzyme, pH 9.0, 30°C, in presence of activator Act
10.35
methanol
-
pH 9.5, 55°C, mutant enzyme S101V
25
methanol
recombinant enzyme, pH 7.4, 30°C, in presence of activator Act
36.83
methanol
-
pH 9.5, 55°C, mutant enzyme A164F
51.24
methanol
-
pH 9.5, 55°C, mutant enzyme T141S
96
methanol
recombinant enzyme, pH 9.0, 30°C, in presence of activator Act
137
methanol
recombinant enzyme mutant D38G, pH 7.4, 30°C, in presence of activator Act, with NADP+
150
methanol
recombinant enzyme, pH 9.0, 30°C, in absence of activator Act
255
methanol
recombinant enzyme, pH 7.4, 30°C, in presence of activator Act
329
methanol
pH 9.5, 37°C, mutant enzyme A164P/A363L
349
methanol
recombinant enzyme, pH 7.4, 30°C, in absence of activator Act
379
methanol
recombinant enzyme mutant D38G, pH 7.4, 30°C, in absence of activator Act, with NADP+
416
methanol
recombinant enzyme, pH 9.0, 30°C, in absence of activator Act
432
methanol
pH 9.5, 37°C, mutant enzyme A363L
440
methanol
pH 9.5, 37°C, mutant enzyme A164P
615
methanol
pH 9.5, 37°C, mutant enzyme E123G
627
methanol
pH 9.5, 37°C, mutant enzyme M163V
636
methanol
pH 9.5, 37°C, wild-type enzyme
733
methanol
recombinant enzyme, pH 7.4, 30°C, in absence of activator Act
847
methanol
recombinant enzyme mutant S98G, pH 7.4, 30°C, in presence of activator Act
1151
methanol
recombinant enzyme mutant S98G, pH 7.4, 30°C, in absence of activator Act
0.0072
n-butanol
pH 9.5, 30°C, recombinant wild-type enzyme
0.0113
n-butanol
pH 9.5, 30°C, recombinant mutant A31V
0.0665
n-butanol
pH 9.5, 30°C, recombinant mutant A169V
0.0759
n-butanol
pH 9.5, 30°C, recombinant mutant A26V/A169V
0.12
n-butanol
pH 9.5, 30°C, recombinant mutant A26V/A31V/A169V
1.09
n-Propanol
-
pH 9.5, 55°C, wild-type enzyme
1.82
n-Propanol
-
pH 9.5, 55°C, mutant enzyme T141S
2.33
n-Propanol
-
pH 9.5, 55°C, mutant enzyme A164F
9.45
n-Propanol
-
pH 9.5, 55°C, mutant enzyme S101V
0.02
NAD+
-
native enzyme, pH 9.5, 50°C
0.04
NAD+
-
recombinant enzyme without added Mg2+, pH 9.5, 50°C
0.04
NAD+
-
recombinant enzyme, pH 9.5, 50°C
0.093
NAD+
pH 9.5, 30°C, recombinant wild-type enzyme
0.2
NAD+
-
S97T mutant enzyme without added Mg2+, pH 9.5, 50°C
0.23
NAD+
-
pH 9.5, 55°C, wild-type enzyme
2.5
NAD+
-
S97G mutant enzyme without added Mg2+, pH 9.5, 50°C
additional information
additional information
-
biphasic kinetics with all alcoholic substrates and NAD+ in the presence of activator protein
-
additional information
additional information
-
3.8 mM and 166 mM, methanol, due to two active sites biphasic kinetics for methanol, ethanol or NAD+ in cell-free extracts, not for formaldehyde
-
additional information
additional information
I3DTM5
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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1.048
butanol
-
pH 9.5, 55°C, wild-type enzyme
0.0335 - 0.509
n-Propanol
0.0006
ethanol
recombinant enzyme, pH 7.4, 30°C, in absence of activator Act
0.0014
ethanol
recombinant enzyme, pH 9.0, 30°C, in absence of activator Act
0.0074
ethanol
recombinant enzyme, pH 7.4, 30°C, in presence of activator Act
0.0143
ethanol
recombinant enzyme, pH 9.0, 30°C, in presence of activator Act
0.0339
ethanol
-
pH 9.5, 55°C, mutant enzyme S101V
0.474
ethanol
-
pH 9.5, 55°C, mutant enzyme T141S
0.523
ethanol
-
pH 9.5, 55°C, mutant enzyme A164F
1.861
ethanol
-
pH 9.5, 55°C, wild-type enzyme
0.00004
methanol
recombinant enzyme, pH 7.4, 30°C, in absence of activator Act
0.0001
methanol
recombinant enzyme mutant D38G, pH 7.4, 30°C, in absence of activator Act, with NADP+
0.00023
methanol
pH 9.5, 37°C, wild-type enzyme
0.00025
methanol
pH 9.5, 37°C, mutant enzyme E123G
0.0003
methanol
recombinant enzyme mutant S98G, pH 7.4, 30°C, in absence of activator Act
0.0003
methanol
recombinant enzyme, pH 7.4, 30°C, in absence of activator Act
0.0003
methanol
recombinant enzyme, pH 9.0, 30°C, in absence of activator Act
0.00035
methanol
pH 9.5, 37°C, mutant enzyme M163V
0.0006
methanol
recombinant enzyme mutant D38G, pH 7.4, 30°C, in presence of activator Act, with NADP+
0.00069
methanol
pH 9.5, 37°C, mutant enzyme A164P
0.0007
methanol
recombinant enzyme mutant S98G, pH 7.4, 30°C, in presence of activator Act
0.0007
methanol
recombinant enzyme, pH 9.0, 30°C, in absence of activator Act
0.0008
methanol
recombinant enzyme, pH 7.4, 30°C, in presence of activator Act
0.00108
methanol
pH 9.5, 37°C, mutant enzyme A164P/A363L
0.00118
methanol
pH 9.5, 37°C, mutant enzyme A363L
0.0016
methanol
pH 9.5, 30°C, recombinant wild-type enzyme
0.0019
methanol
pH 9.5, 30°C, recombinant mutant A31V
0.0028
methanol
recombinant enzyme, pH 9.0, 30°C, in presence of activator Act
0.0048
methanol
pH 9.5, 30°C, recombinant mutant A169V
0.0064
methanol
-
pH 9.5, 55°C, mutant enzyme T141S
0.0068
methanol
pH 9.5, 30°C, recombinant mutant A26V/A169V
0.0068
methanol
recombinant enzyme, pH 7.4, 30°C, in presence of activator Act
0.0092
methanol
-
pH 9.5, 55°C, mutant enzyme A164F
0.0093
methanol
pH 9.5, 30°C, recombinant mutant A26V/A31V/A169V
0.0236
methanol
-
pH 9.5, 55°C, mutant enzyme S101V
0.025
methanol
-
pH 9.5, 55°C, wild-type enzyme
0.0353
methanol
recombinant enzyme, pH 9.0, 30°C, in presence of activator Act
0.0668
methanol
-
pH 9.5, 55°C, wild-type enzyme
0.076
methanol
-
pH 9.5, 55°C, mutant enzyme K46E
0.093
methanol
-
pH 9.5, 55°C, mutant enzyme E396V/K318N
0.58
methanol
-
pH 9.5, 55°C, mutant enzyme K318N
2
methanol
-
pH 9.5, 55°C, mutant enzyme E396V
0.048
n-butanol
pH 9.5, 30°C, recombinant mutant A26V/A31V/A169V
0.05
n-butanol
pH 9.5, 30°C, recombinant mutant A169V
0.066
n-butanol
pH 9.5, 30°C, recombinant mutant A26V/A169V
0.637
n-butanol
pH 9.5, 30°C, recombinant mutant A31V
0.903
n-butanol
pH 9.5, 30°C, recombinant wild-type enzyme
0.0335
n-Propanol
-
pH 9.5, 55°C, mutant enzyme S101V
0.34
n-Propanol
-
pH 9.5, 55°C, mutant enzyme A164F
0.381
n-Propanol
-
pH 9.5, 55°C, mutant enzyme T141S
0.509
n-Propanol
-
pH 9.5, 55°C, wild-type enzyme
0.258
NAD+
pH 9.5, 30°C, recombinant wild-type enzyme
1.648
NAD+
-
pH 9.5, 55°C, wild-type enzyme
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0.001
recombinant wild-type Adh in Escherichia coli suspension cells, pH 7.4, 37°C
0.0014
recombinant wild-type Mdh in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0015
recombinant wild-type Mdh3 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0017
recombinant wild-type Mdh in Escherichia coli suspension cells, pH 7.4, 37°C
0.0018
-
recombinant wild-type Mdh2 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0023
recombinant wild-type Mdh2 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0026
recombinant wild-type Mdh in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0029
recombinant wild-type Adh in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0033
recombinant wild-type Mdh2 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0051
recombinant mutant S97G Mdh in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0057
recombinant mutant S97G Mdh2 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0058
-
recombinant wild-type Mdh2 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.007
-
recombinant wild-type Mdh2 in Escherichia coli suspension cells, pH 7.4, 37°C
0.008 - 4
recombinant wild-type Adh in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C, with addition of Act
0.01
recombinant wild-type Mdh1 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0114
recombinant mutant S97G Mdh2 in Escherichia coli suspension cells, pH 7.4, 37°C
0.014
recombinant mutant S97G Mdh in Escherichia coli suspension cells, pH 7.4, 37°C
0.0167
-
recombinant wild-type Mdh2 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C, with addition of Act
0.021
recombinant mutant S97G Mdh in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C, with addition of Act
0.0213
recombinant wild-type Mdh2 in Escherichia coli suspension cells, pH 7.4, 37°C, with addition of Act
0.023
recombinant wild-type Mdh3 in Escherichia coli suspension cells, pH 7.4, 37°C
0.0273
recombinant wild-type Mdh3 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C, with addition of Act
0.03
recombinant wild-type Mdh2 in Escherichia coli suspension cells, pH 7.4, 37°C
0.045
recombinant wild-type Mdh2 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C, with addition of Act
0.22
recombinant wild-type Mdh2 in Escherichia coli cell-free enzyme extract, pH 9.5, 45°C
1.2
-
enzyme activity in crude extracts of methanol grown cells, fully activated enzyme, enzyme activity is 10fold lower in the absence of activator protein
19.6
-
formaldehyde reductase activity
0.0007
recombinant wild-type Mdh in Escherichia coli suspension cells, pH 7.4, 37°C, with addition of Act
0.0007
recombinant wild-type Mdh2 in Escherichia coli suspension cells, pH 7.4, 37°C
0.003
recombinant wild-type Mdh2 in Escherichia coli suspension cells, pH 7.4, 37°C
0.003
-
recombinant wild-type Mdh2 in Escherichia coli suspension cells, pH 7.4, 37°C
0.0038
-
recombinant wild-type Mdh2 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C
0.0038
-
recombinant wild-type Mdh2 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C, with addition of Act
0.0155
recombinant wild-type Mdh in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C, with addition of Act
0.0155
-
recombinant wild-type Mdh2 in Escherichia coli cell-free enzyme extract, pH 7.4, 37°C, with addition of Act
additional information
I3DTM5
no activity of the recombinant enzyme in Escherichia coli suspension cells
additional information
no activity of the recombinant enzyme in Escherichia coli suspension cells
additional information
no activity of the recombinant enzyme in Escherichia coli suspension cells
additional information
no activity of the recombinant enzyme in Escherichia coli suspension cells
additional information
no activity of the recombinant enzyme in Escherichia coli suspension cells
additional information
no activity of the recombinant enzyme in Escherichia coli suspension cells
additional information
-
no activity of the recombinant enzyme in Escherichia coli suspension cells
additional information
-
no activity of the recombinant enzyme in Escherichia coli suspension cells
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evolution
-
strain MGA3 contains three isozymes that belong to the type III Fe-NAD+-dependent alcohol dehydrogenases, but show a distinct substrate specificity and major differences with respect to transcriptional regulation of the paralogous genes
evolution
-
strain PB1 contains three isozymes that belong to the type III Fe-NAD+-dependent alcohol dehydrogenases, but show a distinct substrate specificity and major differences with respect to transcriptional regulation of the paralogous genes
evolution
Mdh2 is a group III Adh
evolution
the enzyme belongs to the type III alcohol dehydrogenase (Adh) family
evolution
the formaldehyde reduction activity of the enzyme is successfully improved by directed evolution and screening, which might potentially be useful for the conversion of CO2 to methanol
evolution
-
strain MGA3 contains three isozymes that belong to the type III Fe-NAD+-dependent alcohol dehydrogenases, but show a distinct substrate specificity and major differences with respect to transcriptional regulation of the paralogous genes
-
evolution
-
strain PB1 contains three isozymes that belong to the type III Fe-NAD+-dependent alcohol dehydrogenases, but show a distinct substrate specificity and major differences with respect to transcriptional regulation of the paralogous genes
-
evolution
-
Mdh2 is a group III Adh
-
evolution
-
the formaldehyde reduction activity of the enzyme is successfully improved by directed evolution and screening, which might potentially be useful for the conversion of CO2 to methanol
-
evolution
-
strain MGA3 contains three isozymes that belong to the type III Fe-NAD+-dependent alcohol dehydrogenases, but show a distinct substrate specificity and major differences with respect to transcriptional regulation of the paralogous genes
-
evolution
-
strain PB1 contains three isozymes that belong to the type III Fe-NAD+-dependent alcohol dehydrogenases, but show a distinct substrate specificity and major differences with respect to transcriptional regulation of the paralogous genes
-
evolution
-
the enzyme belongs to the type III alcohol dehydrogenase (Adh) family
-
metabolism
-
assimilation of methanol into central metabolism, overview
metabolism
-
methanol dehydrogenase, is a crucial enzyme for utilizing methane and methanol as carbon and energy sources in methylotrophy and synthetic methylotrophy
metabolism
-
methanol oxidation catalyzed by methanol dehydrogenase is one of the key steps in methanol utilization in bacterial methylotrophy
metabolism
the enzyme catalyzes a key step for ethanol production in bacterial methylotrophy and a key step for both toxic formaldehyde elimination
metabolism
-
methanol oxidation catalyzed by methanol dehydrogenase is one of the key steps in methanol utilization in bacterial methylotrophy
-
metabolism
-
the enzyme catalyzes a key step for ethanol production in bacterial methylotrophy and a key step for both toxic formaldehyde elimination
-
physiological function
-
biological significance of Mdh for methanol oxidation during methylotrophic growth and biological role of the enzyme as part of a formaldehyde detoxification system in the methanol consuming cells
physiological function
-
biological significance of Mdh for methanol oxidation during methylotrophic growth and biological role of the enzyme as part of a formaldehyde detoxification system in the methanol consuming cells
-
physiological function
-
biological significance of Mdh for methanol oxidation during methylotrophic growth and biological role of the enzyme as part of a formaldehyde detoxification system in the methanol consuming cells
-
additional information
in nature, methanol dehydrogenase (Mdh), which converts methanol to formaldehyde, highly favors the reverse reaction, efficient coupling with the irreversible sequestration of formaldehyde by 3-hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloseisomerase (Phi) serves as the key driving force to pull the pathway equilibrium toward central metabolism. An emerging strategy to promote efficient substrate channeling is to spatially organize pathway enzymes in an engineered assembly to provide kinetic driving forces that promote carbon flux in a desirable direction. A scaffoldless, self-assembly strategy is applied to organize Mdh, Hps, and Phi into an engineered supramolecular enzyme complex using an SH3-ligand interaction pair, which enhances methanol conversion to fructose-6-phosphate. An NADH sink is created using Escherichia coli lactate dehydrogenase as an NADH scavenger, thereby preventing reversible formaldehyde reduction, to increase methanol consumption. Combination of the two strategies improves in vitro fructose 6-phosphate production by 97fold compared with unassembled enzymes. The beneficial effect of supramolecular enzyme assembly is also realized in vivo as the engineered enzyme assembly improves whole-cell methanol consumption rate by ninefold. This approach ultimately allows direct coupling of enhanced fructose 6-phosphate synthesis with other metabolic engineering strategies for the production of many desired metabolites from methanol
additional information
-
in nature, methanol dehydrogenase (Mdh), which converts methanol to formaldehyde, highly favors the reverse reaction, efficient coupling with the irreversible sequestration of formaldehyde by 3-hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloseisomerase (Phi) serves as the key driving force to pull the pathway equilibrium toward central metabolism. An emerging strategy to promote efficient substrate channeling is to spatially organize pathway enzymes in an engineered assembly to provide kinetic driving forces that promote carbon flux in a desirable direction. A scaffoldless, self-assembly strategy is applied to organize Mdh, Hps, and Phi into an engineered supramolecular enzyme complex using an SH3-ligand interaction pair, which enhances methanol conversion to fructose-6-phosphate. An NADH sink is created using Escherichia coli lactate dehydrogenase as an NADH scavenger, thereby preventing reversible formaldehyde reduction, to increase methanol consumption. Combination of the two strategies improves in vitro fructose 6-phosphate production by 97fold compared with unassembled enzymes. The beneficial effect of supramolecular enzyme assembly is also realized in vivo as the engineered enzyme assembly improves whole-cell methanol consumption rate by ninefold. This approach ultimately allows direct coupling of enhanced fructose 6-phosphate synthesis with other metabolic engineering strategies for the production of many desired metabolites from methanol
-
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A363L
5.1fold increase in kcat/Km as compared to wild-type enzyme
D100N
-
strongly reduced NAD+-binding, no activity
D88N
-
only minor effects on activity
E123G
1.1fold increase in kcat/Km as compared to wild-type enzyme
F213V/F289L
the mutant enzyme shows 25.3fold higher catalytic efficiency (kcat/Km) than wild type enzyme. It converts 5.9fold more formaldehyde to methanol in vitro than the wild type enzyme
F213V/F289L/F356S
the mutant enzyme shows 52.8fold higher catalytic efficiency (kcat/Km) than wild type enzyme. It converts 6.4fold more formaldehyde to methanol in vitro than the wild type enzyme
G13A
-
only minor effects on activity
G15A
-
only minor effects on activity
G95A
-
impaired cofactor binding, low acitivity
K103R
-
strongly reduced NAD+-binding, no activity
M163V
1.5fold increase in kcat/Km as compared to wild-type enzyme
S101G
site-directed mutagenesis, the mutant shows altered kinetics, reduced activity, and altered pH-dependency compared to the wild-type enzyme, overview
S97T
-
impaired cofactor binding, much higher acitivity than the wild type enzyme, no activation with ACT protein
S98G
site-directed mutagenesis, the mutant shows altered kinetics, reduced activity, and altered pH-dependency compared to the wild-type enzyme, overview
A363L
-
5.1fold increase in kcat/Km as compared to wild-type enzyme
-
E123G
-
1.1fold increase in kcat/Km as compared to wild-type enzyme
-
M163V
-
1.5fold increase in kcat/Km as compared to wild-type enzyme
-
F213V/F289L
-
the mutant enzyme shows 25.3fold higher catalytic efficiency (kcat/Km) than wild type enzyme. It converts 5.9fold more formaldehyde to methanol in vitro than the wild type enzyme
-
F213V/F289L/F356S
-
the mutant enzyme shows 52.8fold higher catalytic efficiency (kcat/Km) than wild type enzyme. It converts 6.4fold more formaldehyde to methanol in vitro than the wild type enzyme
-
S101G
-
site-directed mutagenesis, the mutant shows altered kinetics, reduced activity, and altered pH-dependency compared to the wild-type enzyme, overview
-
S98G
-
site-directed mutagenesis, the mutant shows altered kinetics, reduced activity, and altered pH-dependency compared to the wild-type enzyme, overview
-
A169C
site-directed mutagenesis
A169I
site-directed mutagenesis
A169L
site-directed mutagenesis
A169M
site-directed mutagenesis
A169P
site-directed mutagenesis
A169V
from library screening, mutant CT1-2, mutant variants CT1-2, CT2-1, and CT4-1 show 5 to 10fold reduced specific activity towards ethanol and 6 to 8fold reduced for propanol compared to wild-type
A26V
site-directed mutagenesis, mutant CT2-2, the mutation A26V alone demolishes Mdh activity, inactive mutant
A26V/A169V
site-directed mutagenesis, mutant CT2-1, synergistic effect of mutation A26V and A169V in enzyme function increasing the activity. Mutant variants CT1-2, CT2-1, and CT4-1 show 5 to 10fold reduced specific activity towards ethanol and 6 to 8fold reduced for propanol compared to wild-type
A26V/A31V/A169V
site-directed mutagenesis, mutant CT4-1. Engineering of a mutant enzyme chimeric variant CT4-1 of Mdh2 that shows a 6fold higher Kcat/Km for methanol and 10fold lower Kcat/Km for n-butanol. CT4-1 represents an NAD-dependent Mdh with much improved catalytic efficiency and specificity toward methanol compared with the existing NAD-dependent Mdhs with or without ACT activation. Development of automatic high throughput screening (HTS) for Mdh evolution, overview. Mutant variants CT1-2, CT2-1, and CT4-1 show 5 to 10fold reduced specific activity towards ethanol and 6 to 8fold reduced for propanol compared to wild-type. CT4-1 significantly improves its methanol over C2 to C4 alcohol activity ratio compared to wild-type
A31V
from library screening, mutant CT1-1
A169L
-
site-directed mutagenesis
-
A169V
-
from library screening, mutant CT1-2, mutant variants CT1-2, CT2-1, and CT4-1 show 5 to 10fold reduced specific activity towards ethanol and 6 to 8fold reduced for propanol compared to wild-type
-
A26V
-
site-directed mutagenesis, mutant CT2-2, the mutation A26V alone demolishes Mdh activity, inactive mutant
-
A31V
-
from library screening, mutant CT1-1
-
A164F
-
mutation improves the specific activity of the enzyme toward methanol compared to that of the wild-type enzyme. Mutant shows a slightly higher turnover rate than that of wild-type, although the KM value is increased compared to that of wild-type
S101V
-
mutation improves the specific activity of the enzyme toward methanol compared to that of the wild-type enzyme. Mutant shows a slightly higher turnover rate than that of wild-type, although the KM value is increased compared to that of wild-type
T141S
-
mutation improves the specific activity of the enzyme toward methanol compared to that of the wild-type enzyme. Mutant shows a slightly higher turnover rate than that of wild-type, although the KM value is increased compared to that of wild-type
A164F
-
mutation improves the specific activity of the enzyme toward methanol compared to that of the wild-type enzyme. Mutant shows a slightly higher turnover rate than that of wild-type, although the KM value is increased compared to that of wild-type
-
S101V
-
mutation improves the specific activity of the enzyme toward methanol compared to that of the wild-type enzyme. Mutant shows a slightly higher turnover rate than that of wild-type, although the KM value is increased compared to that of wild-type
-
T141S
-
mutation improves the specific activity of the enzyme toward methanol compared to that of the wild-type enzyme. Mutant shows a slightly higher turnover rate than that of wild-type, although the KM value is increased compared to that of wild-type
-
A164P
3fold increase in kcat/Km as compared to wild-type enzyme
A164P
4.7fold increase in kcat/Km as compared to wild-type enzyme
D38G
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D38G
site-directed mutagenesis, the mutant is active with NADP+ and NAD+ in contrast to the wild-type enzyme
D41G
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D41G
site-directed mutagenesis, the mutant is active with NADP+ and NAD+ in contrast to the wild-type enzyme, it shows increased activity compared to the wild-type enzyme
S97G
-
impaired cofactor binding, much higher acitivity than the wild type enzyme, no activation with ACT protein
S97G
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
S97G
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
A164P
-
3fold increase in kcat/Km as compared to wild-type enzyme
-
A164P
-
4.7fold increase in kcat/Km as compared to wild-type enzyme
-
D38G
-
site-directed mutagenesis, the mutant is active with NADP+ and NAD+ in contrast to the wild-type enzyme
-
D38G
-
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
-
D41G
-
site-directed mutagenesis, the mutant is active with NADP+ and NAD+ in contrast to the wild-type enzyme, it shows increased activity compared to the wild-type enzyme
-
D41G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
S97G
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
-
S97G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
E396V
-
mutant enzyme has superior methanol conversion efficiency, with 79fold improvements compared to the wild-type
E396V
-
mutant enzyme shows high activity, particularly at very low methanol concentrations
K318N
-
mutant enzyme has superior methanol conversion efficiency, with 23fold improvements compared to the wild-type
K318N
-
mutant enzyme shows high activity, particularly at very low methanol concentrations
K46E
-
mutant enzyme has superior methanol conversion efficiency, with 3fold improvements compared to the wild-type
K46E
-
mutant enzyme shows high activity, particularly at very low methanol concentrations
additional information
construction of multienzyme supramolecular complexes, which self-assemble into spatially defined architectures, to improve the efficiency of cascade reactions. Engineered supramolecular enzyme assemblies enhance hexose 6-phosphate and fructose 6-phosphate production and can be similarly created as a kinetic trap to enable fast and efficient methanol utilization, method, overview. Clustering Mdh3 with a bifunctional Hps-Phi fusion, further improves fructose 6-phosphate production, resulting in an overall 50fold improvement over the uncomplexed enzyme mixture. Compared with the unassembled enzyme system, a much lower level of formaldehyde is detected and only a small amount of hexose 6-phosphate is accumulated, indicating the effective channeling of formaldehyde toward fructose 6-phosphate by the supramolecular enzyme complex due to improved molecular proximity
additional information
I3DTM5
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
I3DTM5
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), up to 40% incorporation of methanol into central metabolites is achieved, system evaluation, overview
additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), up to 40% incorporation of methanol into central metabolites is achieved, system evaluation, overview
additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), up to 40% incorporation of methanol into central metabolites is achieved, system evaluation, overview
additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), up to 40% incorporation of methanol into central metabolites is achieved, system evaluation, overview
additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), up to 40% incorporation of methanol into central metabolites is achieved, system evaluation, overview
additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), up to 40% incorporation of methanol into central metabolites is achieved, system evaluation, overview
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), up to 40% incorporation of methanol into central metabolites is achieved, system evaluation, overview
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
-
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), up to 40% incorporation of methanol into central metabolites is achieved, system evaluation, overview
-
additional information
-
construction of multienzyme supramolecular complexes, which self-assemble into spatially defined architectures, to improve the efficiency of cascade reactions. Engineered supramolecular enzyme assemblies enhance hexose 6-phosphate and fructose 6-phosphate production and can be similarly created as a kinetic trap to enable fast and efficient methanol utilization, method, overview. Clustering Mdh3 with a bifunctional Hps-Phi fusion, further improves fructose 6-phosphate production, resulting in an overall 50fold improvement over the uncomplexed enzyme mixture. Compared with the unassembled enzyme system, a much lower level of formaldehyde is detected and only a small amount of hexose 6-phosphate is accumulated, indicating the effective channeling of formaldehyde toward fructose 6-phosphate by the supramolecular enzyme complex due to improved molecular proximity
-
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
-
additional information
engineering of a mutant enzyme variants results in enzymes with reduced activity with n-butanol and increased activity with methanol compared to wild-type
additional information
-
engineering of a mutant enzyme variants results in enzymes with reduced activity with n-butanol and increased activity with methanol compared to wild-type
additional information
-
engineering of a mutant enzyme variants results in enzymes with reduced activity with n-butanol and increased activity with methanol compared to wild-type
-
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
-
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
-
additional information
-
Engineering the biological conversion of methanol to specialty chemicals in Escherichia coli strain BW25113 DELTAfrmA by expressing the methanol dehydrogenase from Bacillus stearothermophilus and and ribulose monophosphate (RuMP) pathway enzymes from Bacillus methanolicus. The recombinant Escherichia coli strain converts methanol into biomass components. Effective methanol assimilation by the engineered Escherichia coli strain can be enhanced in the presence of small amounts of yeast extract or tryptone. Method, overview
additional information
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utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
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utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
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additional information
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
additional information
-
utilization of methanol in Escherichia coli is allowed by the implementation of NAD-dependent methanol dehydrogenase and the establishment of the ribulose monophosphate cycle by expressing the genes for hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi), system evaluation, overview
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Arfman, N.; Watling, E.M.; Clement, W.; Van Oosterwijk, R.J.; De Vries, G.E.; Harder, W.; Attwood, M.M.; Dijkhuizen, L.
Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme
Arch. Microbiol.
152
280-288
1989
Bacillus methanolicus
brenda
Arfman, N.; Dijkhuizen, L.
Methanol dehydrogenase from thermotolerant methylotroph Bacillus C1
Methods Enzymol.
188
223-226
1990
Bacillus methanolicus
brenda
Vonck, J.; Arfman, N.; De Vries, G.E.; Van Beeumen, J.; Van Bruggen, E.F.J.; Dijkhuizen, L.
Electron microscopic analysis and biochemical characterization of a novel methanol dehydrogenase from the thermotolerant Bacillus sp. C1
J. Biol. Chem.
266
3949-3954
1991
Bacillus methanolicus
brenda
Arfman, N.; Van Beeumen, J.; De Vries, G.E.; Harder, W.; Dijkhuizen, L.
Purification and characterization of an activator protein for methanol dehydrogenase from thermotolerant Bacillus sp.
J. Biol. Chem.
266
3955-3960
1991
Bacillus methanolicus
brenda
Arfman, N.; de Vries, K.J.; Moezelaar, H.R.; Attwood, M.M.; Robinson, G.K.; van Geel, M.; Dijkhuizen, L.
Environmental regulation of alcohol metabolism in thermotolerant methylotrophic Bacillus strains
Arch. Microbiol.
157
272-278
1992
Bacillus methanolicus
brenda
Arfman, N.; Hektor, H.J.; Bystrykh, L.V.; Govorukhina, N.I.; Dijkhuizen, L.; Frank, J.
Properties of an NAD(H)-containing methanol dehydrogenase and its activator protein from Bacillus methanolicus
Eur. J. Biochem.
244
426-433
1997
Bacillus methanolicus
brenda
Kloosterman, H.; Vrijbloed, J.W.; Dijkhuizen, L.
Molecular, biochemical, and functional characterization of a Nudix hydrolase protein that stimulates the activity of a nicotinoprotein alcohol dehydrogenase
J. Biol. Chem.
277
34785-34792
2002
Bacillus methanolicus, Bacillus methanolicus C1
brenda
Hektor, H.J.; Kloosterman, H.; Dijkhuizen, L.
Identification of a magnesium-dependent NAD(P)(H)-binding domain in the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus
J. Biol. Chem.
277
46966-46973
2002
Bacillus methanolicus
brenda
Jewell, T.; Huston, S.L.; Nelson, D.C.
Methylotrophy in freshwater Beggiatoa alba strains
Appl. Environ. Microbiol.
74
5575-5578
2008
Beggiatoa alba (B3FR84), Beggiatoa alba
brenda
Krog, A.; Heggeset, T.M.; Mueller, J.E.; Kupper, C.E.; Schneider, O.; Vorholt, J.A.; Ellingsen, T.E.; Brautaset, T.
Methylotrophic Bacillus methanolicus encodes two chromosomal and one plasmid born NAD+ dependent methanol dehydrogenase paralogs with different catalytic and biochemical properties
PLoS ONE
8
e59188
2013
Bacillus methanolicus, Bacillus methanolicus PB1, Bacillus methanolicus MGA3
brenda
Wu, T.Y.; Chen, C.T.; Liu, J.T.; Bogorad, I.W.; Damoiseaux, R.; Liao, J.C.
Characterization and evolution of an activator-independent methanol dehydrogenase from Cupriavidus necator N-1
Appl. Microbiol. Biotechnol.
100
4969-4983
2016
Cupriavidus necator (F8GNE5), Cupriavidus necator, Cupriavidus necator N-1 (F8GNE5), Cupriavidus necator N-1
brenda
Ochsner, A.M.; Mueller, J.E.; Mora, C.A.; Vorholt, J.A.
In vitro activation of NAD-dependent alcohol dehydrogenases by Nudix hydrolases is more widespread than assumed
FEBS Lett.
588
2993-2999
2014
Bacillus methanolicus (I3DTM5), Bacillus methanolicus (I3E2P9), Bacillus methanolicus, Bacillus methanolicus MGA3 (I3DTM5), Bacillus methanolicus MGA3 (I3E2P9)
brenda
Mueller, J.E.; Meyer, F.; Litsanov, B.; Kiefer, P.; Potthoff, E.; Heux, S.; Quax, W.J.; Wendisch, V.F.; Brautaset, T.; Portais, J.C.; Vorholt, J.A.
Engineering Escherichia coli for methanol conversion
Metab. Eng.
28
190-201
2015
Weizmannia coagulans, Desulfitobacterium hafniense, Lysinibacillus fusiformis, Desulfofundulus kuznetsovii, Lysinibacillus sphaericus (B1HX72), Bacillus methanolicus (I3DTM5), Bacillus methanolicus (I3DTP7), Bacillus methanolicus (I3DVX6), Bacillus methanolicus (I3DX19), Bacillus methanolicus (I3E2P9), Bacillus methanolicus (I3E949), Bacillus methanolicus, Desulfofundulus kuznetsovii MGA3, Lysinibacillus fusiformis ZC1, Desulfitobacterium hafniense Y51, Bacillus methanolicus PB1 (I3DTP7), Bacillus methanolicus PB1 (I3DVX6), Bacillus methanolicus PB1 (I3DX19), Weizmannia coagulans 36D1, Bacillus methanolicus MGA3 (I3DTM5), Bacillus methanolicus MGA3 (I3E2P9), Bacillus methanolicus MGA3 (I3E949)
brenda
Whitaker, W.; Jones, J.; Bennett, R.; Gonzalez, J.; Vernacchio, V.; Collins, S.; Palmer, M.; Schmidt, S.; Antoniewicz, M.; Koffas, M.; Papoutsakis, E.
Engineering the biological conversion of methanol to specialty chemicals in Escherichia coli
Metab. Eng.
39
49-59
2017
Geobacillus stearothermophilus
brenda
Price, J.; Chen, L.; Whitaker, W.; Papoutsakis, E.; Chen, W.
Scaffoldless engineered enzyme assembly for enhanced methanol utilization
Proc. Natl. Acad. Sci. USA
113
12691-12696
2016
Bacillus methanolicus (I3E949), Bacillus methanolicus MGA3 (I3E949)
brenda
Zhang, W.; Zhang, T.; Song, M.; Dai, Z.; Zhang, S.; Xin, F.; Dong, W.; Ma, J.; Jiang, M.
Metabolic engineering of Escherichia coli for high yield production of succinic acid driven by methanol
ACS Synth. Biol.
7
2803-2811
2018
Bacillus methanolicus (I3E2P9), Bacillus methanolicus, Bacillus methanolicus MGA3 (I3E2P9)
brenda
Roth, T.B.; Woolston, B.M.; Stephanopoulos, G.; Liu, D.R.
Phage-assisted evolution of Bacillus methanolicus methanol dehydrogenase 2
ACS Synth. Biol.
8
796-806
2019
Bacillus methanolicus (I3E2P9), Bacillus methanolicus, Bacillus methanolicus ATCC 53907 (I3E2P9)
brenda
Lee, J.Y.; Park, S.H.; Oh, S.H.; Lee, J.J.; Kwon, K.K.; Kim, S.J.; Choi, M.; Rha, E.; Lee, H.; Lee, D.H.; Sung, B.H.; Yeom, S.J.; Lee, S.G.
Discovery and biochemical characterization of a methanol dehydrogenase from Lysinibacillus xylanilyticus
Front. Bioeng. Biotechnol.
8
67
2020
Lysinibacillus xylanilyticus, Lysinibacillus xylanilyticus KCTC 13423
brenda
Le, T.K.; Ju, S.B.; Lee, H.W.; Lee, J.Y.; Oh, S.H.; Kwon, K.K.; Sung, B.H.; Lee, S.G.; Yeom, S.J.
Biosensor-based directed evolution of methanol dehydrogenase from Lysinibacillus xylanilyticus
Int. J. Mol. Sci.
22
1471
2021
Lysinibacillus xylanilyticus
brenda
Yi, J.; Lee, J.; Sung, B.H.; Kang, D.K.; Lim, G.; Bae, J.H.; Lee, S.G.; Kim, S.C.; Sohn, J.H.
Development of Bacillus methanolicus methanol dehydrogenase with improved formaldehyde reduction activity
Sci. Rep.
8
12483
2018
Bacillus methanolicus (P31005), Bacillus methanolicus, Bacillus methanolicus C1 (P31005)
brenda