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
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methylotrophy
- methylamine
-
paracoccus
-
lanthanide
- methylophilus
- hyphomicrobium
- methanolicus
- methylomonas
- methylosinus
- methylococcus
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methane-oxidizing
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methanol-grown
- trichosporium
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lanthanide-dependent
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pqq-dependent
- methylomicrobium
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pink-pigmented
-
pyrrolo-quinoline
-
rump
- methylocystis
- methylophaga
- methylobacter
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xoxf-type
-
pqq-containing
- organophilum
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phyllosphere
-
quinone-dependent
- methylacidiphilum
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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
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General Information
General Information on EC 1.1.1.244 - methanol dehydrogenase
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evolution
metabolism
physiological function
additional information
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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
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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 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
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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 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
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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
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evolution
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the enzyme belongs to the type III alcohol dehydrogenase (Adh) family
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assimilation of methanol into central metabolism, overview
metabolism
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methanol dehydrogenase, is a crucial enzyme for utilizing methane and methanol as carbon and energy sources in methylotrophy and synthetic methylotrophy
metabolism
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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
Lysinibacillus xylanilyticus KCTC 13423
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methanol oxidation catalyzed by methanol dehydrogenase is one of the key steps in methanol utilization in bacterial methylotrophy
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metabolism
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the enzyme catalyzes a key step for ethanol production in bacterial methylotrophy and a key step for both toxic formaldehyde elimination
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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
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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
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physiological function
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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
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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
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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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