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1.1.1.244: methanol dehydrogenase

This is an abbreviated version!
For detailed information about methanol dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.244

Reaction

methanol
+
NAD+
=
formaldehyde
+
NADH
+
H+

Synonyms

activator-independent methanol dehydrogenase, ADH, BFZC1_05383, BsMdh, Bsph_4187, CNE_2c13570, dehydrogenase, methanol, group III NAD-dependent alcohol dehydrogenase, lxmdh, MDH, Mdh1, MDH2, Mdh3, MEDH, methanol dehydrogenase 2, More, NAD+ dependent methanol dehydrogenase, NAD-dependent MDH, NAD-dependent methanol dehydrogenase, XoxF

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.244 methanol dehydrogenase

Engineering

Engineering on EC 1.1.1.244 - methanol dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A164P
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
I3DTM5, I3E2P9
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
I3DTM5, I3E2P9
site-directed mutagenesis, the mutant shows altered kinetics, reduced activity, and altered pH-dependency compared to the wild-type enzyme, overview
A164P
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
E396V
K318N
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
-
additional information