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
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1.1.1.244
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methylobacterium
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formaldehyde
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quinone
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methane
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methanotrophs
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pqq
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extorquens
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quinoproteins
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denitrificans
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methylotrophy
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methylamine
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paracoccus
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lanthanide
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methylophilus
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hyphomicrobium
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methanolicus
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methylomonas
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methylosinus
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methylococcus
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methane-oxidizing
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methanol-grown
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trichosporium
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lanthanide-dependent
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pqq-dependent
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methylomicrobium
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pink-pigmented
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pyrrolo-quinoline
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rump
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methylocystis
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methylophaga
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methylobacter
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xoxf-type
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pqq-containing
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organophilum
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phyllosphere
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quinone-dependent
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methylacidiphilum
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rare-earth
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ch3oh
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dye-linked
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biotechnology
- 1.1.1.244
- methylobacterium
- formaldehyde
- quinone
- methane
- methanotrophs
- pqq
- extorquens
-
quinoproteins
- denitrificans
-
methylotrophy
- methylamine
-
paracoccus
-
lanthanide
- methylophilus
- hyphomicrobium
- methanolicus
- methylomonas
- methylosinus
- methylococcus
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methane-oxidizing
-
methanol-grown
- trichosporium
-
lanthanide-dependent
-
pqq-dependent
- methylomicrobium
-
pink-pigmented
-
pyrrolo-quinoline
-
rump
- methylocystis
- methylophaga
- methylobacter
-
xoxf-type
-
pqq-containing
- organophilum
-
phyllosphere
-
quinone-dependent
- methylacidiphilum
-
rare-earth
- ch3oh
-
dye-linked
- biotechnology
Reaction
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
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Engineering
Engineering on EC 1.1.1.244 - methanol dehydrogenase
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A164P
A363L
5.1fold increase in kcat/Km as compared to wild-type enzyme
D38G
D41G
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
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
S97G
S97T
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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
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5.1fold increase in kcat/Km as compared to wild-type enzyme
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E123G
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1.1fold increase in kcat/Km as compared to wild-type enzyme
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M163V
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1.5fold increase in kcat/Km as compared to wild-type enzyme
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F213V/F289L
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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
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F213V/F289L/F356S
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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
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D38G
D41G
S101G
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site-directed mutagenesis, the mutant shows altered kinetics, reduced activity, and altered pH-dependency compared to the wild-type enzyme, overview
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S97G
S98G
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site-directed mutagenesis, the mutant shows altered kinetics, reduced activity, and altered pH-dependency compared to the wild-type enzyme, overview
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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
A169V
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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
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A26V
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site-directed mutagenesis, mutant CT2-2, the mutation A26V alone demolishes Mdh activity, inactive mutant
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A164F
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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
K46E
S101V
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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
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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
Lysinibacillus xylanilyticus KCTC 13423
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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
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S101V
Lysinibacillus xylanilyticus KCTC 13423
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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
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T141S
Lysinibacillus xylanilyticus KCTC 13423
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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
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additional information
A164P
4.7fold increase in kcat/Km as compared to wild-type enzyme
site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
D38G
I3DTM5, I3E2P9
site-directed mutagenesis, the mutant is active with NADP+ and NAD+ in contrast to the wild-type enzyme
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D41G
I3DTM5, I3E2P9
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
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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
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3fold increase in kcat/Km as compared to wild-type enzyme
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A164P
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4.7fold increase in kcat/Km as compared to wild-type enzyme
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site-directed mutagenesis, the mutant is active with NADP+ and NAD+ in contrast to the wild-type enzyme
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D38G
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site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme
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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
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D41G
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
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S97G
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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mutant enzyme has superior methanol conversion efficiency, with 79fold improvements compared to the wild-type
E396V
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mutant enzyme shows high activity, particularly at very low methanol concentrations
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mutant enzyme has superior methanol conversion efficiency, with 23fold improvements compared to the wild-type
K318N
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mutant enzyme shows high activity, particularly at very low methanol concentrations
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mutant enzyme has superior methanol conversion efficiency, with 3fold improvements compared to the wild-type
K46E
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mutant enzyme shows high activity, particularly at very low methanol concentrations
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
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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
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
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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
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additional information
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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
-
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
-