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Literature summary for 1.1.2.7 extracted from

  • Kalyuzhnaya, M.G.; Hristova, K.R.; Lidstrom, M.E.; Chistoserdova, L.
    Characterization of a novel methanol dehydrogenase in representatives of Burkholderiales: implications for environmental detection of methylotrophy and evidence for convergent evolution (2008), J. Bacteriol., 190, 3817-3823.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
NH4Cl essential activator Methyloversatilis universalis
NH4Cl essential activator Methylibium petroleiphilum

Cloned(Commentary)

Cloned (Comment) Organism
gene mdh2, DNA and amino acid sequence determination and analysis, phylogenetic analysis Methyloversatilis universalis
gene mdh2, DNA and amino acid sequence determination and analysis, phylogenetic analysis Methylibium petroleiphilum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
ethanol pH 7.5, 22°C Methylibium petroleiphilum
0.01
-
methanol pH 7.5, 22°C Methyloversatilis universalis
0.01
-
n-butanol pH 7.5, 22°C Methylibium petroleiphilum
0.05
-
ethanol pH 7.5, 22°C Methyloversatilis universalis
0.09
-
n-Propanol pH 7.5, 22°C Methylibium petroleiphilum
0.29
-
methanol pH 7.5, 22°C Methylibium petroleiphilum
0.5
-
n-butanol pH 7.5, 22°C Methyloversatilis universalis
0.5
-
n-Propanol pH 7.5, 22°C Methyloversatilis universalis

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Methyloversatilis universalis
-
-
periplasm
-
Methylibium petroleiphilum
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Methyloversatilis universalis methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria ?
-
?
additional information Methylibium petroleiphilum methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria ?
-
?
additional information Methyloversatilis universalis FAM5 methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria ?
-
?

Organism

Organism UniProt Comment Textmining
Methylibium petroleiphilum
-
gene mdh2, the organism lacks gene mxaFI, which encodes the wide-spread dimeric methanol dehydrogenase
-
Methyloversatilis universalis
-
gene mdh2, the organism lacks gene mxaFI, which encodes the wide-spread dimeric methanol dehydrogenase
-
Methyloversatilis universalis FAM5
-
gene mdh2, the organism lacks gene mxaFI, which encodes the wide-spread dimeric methanol dehydrogenase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ethanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methyloversatilis universalis acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
?
ethanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methylibium petroleiphilum acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
?
ethanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methyloversatilis universalis FAM5 acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
?
methanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methyloversatilis universalis formaldehyde + reduced 2,6-dichlorophenolindophenol
-
?
methanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methylibium petroleiphilum formaldehyde + reduced 2,6-dichlorophenolindophenol
-
?
methanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methyloversatilis universalis FAM5 formaldehyde + reduced 2,6-dichlorophenolindophenol
-
?
additional information methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria Methyloversatilis universalis ?
-
?
additional information methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria Methylibium petroleiphilum ?
-
?
additional information methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria Methyloversatilis universalis FAM5 ?
-
?
n-butanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methyloversatilis universalis butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
?
n-butanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methylibium petroleiphilum butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
?
n-butanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methyloversatilis universalis FAM5 butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
?
n-propanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methyloversatilis universalis propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
?
n-propanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methylibium petroleiphilum propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
?
n-propanol + 2,6-dichlorophenolindophenol reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate Methyloversatilis universalis FAM5 propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
?

Subunits

Subunits Comment Organism
monomer in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methyloversatilis universalis strain FAM5 is a monosubunit protein Methyloversatilis universalis
More in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methylibium petroleiphilum strain PM1 is a monosubunit protein Methylibium petroleiphilum

Synonyms

Synonyms Comment Organism
MDH2 Mdh2 is a type I alcohol dehydrogenase Methylibium petroleiphilum
More Mdh2 is a type I alcohol dehydrogenase Methyloversatilis universalis
pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenase
-
Methyloversatilis universalis
pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenase
-
Methylibium petroleiphilum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Methyloversatilis universalis
22
-
assay at room temperature Methylibium petroleiphilum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Methyloversatilis universalis
7.5
-
assay at Methylibium petroleiphilum

Cofactor

Cofactor Comment Organism Structure
phenazine methosulfate mediates reduction of 2,6-dichlorophenol-indophenol Methyloversatilis universalis
phenazine methosulfate mediates reduction of 2,6-dichlorophenolindophenol Methylibium petroleiphilum
pyrroloquinoline quinone dependent on Methyloversatilis universalis
pyrroloquinoline quinone dependent on Methylibium petroleiphilum