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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
medh-pd,
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quinoprotein methanol dehydrogenase
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methanol dehydrogenase
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methanol + 2 ferricytochrome c551i = formaldehyde + 2 ferrocytochrome c551i + 2 H+
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methanol:ferricytochrome c551i oxidoreductase
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butanol + N,N,N',N'-tetramethyl-4-phenylenediamine
butyraldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
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-
?
ethanol + N,N,N',N'-tetramethyl-4-phenylenediamine
acetaldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
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-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
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-
?
methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
methanol + N,N,N',N'-tetramethyl-4-phenylenediamine
formaldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
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-
?
methanol + nitroblue tetrazolium
formaldehyde + reduced nitroblue tetrazolium
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-
-
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
phenazine ethosulfate is a two-electron acceptor
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?
propanol + N,N,N',N'-tetramethyl-4-phenylenediamine
propionaldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
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-
?
additional information
?
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methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
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-
?
methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
the primary electron acceptor of MEDH-PD is cytochrome c-551i
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?
additional information
?
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interaction of the enzyme with cytochrome c551i, and electron transfer from reduced pyrroloquinoline quinone to the cytochrome, interface structure, modelling, overview
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?
additional information
?
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interaction of the enzyme with cytochrome c551i, and electron transfer from reduced pyrroloquinoline quinone to the cytochrome, interface structure, modelling, overview
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?
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methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
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?
methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
the primary electron acceptor of MEDH-PD is cytochrome c-551i
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-
?
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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non-covalently bound
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Ca2+
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Ca2+
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increases enzyme thermal stability, Ca2+ has a structural role
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cyanide
suppresses the peculiar endogenous reaction of methanol dehydrogenase, and is also both an activator of substrate-dependent activity and a competitive inhibitor with respect to methanol, the two activities correspond to two distinct binding sites for cyanide, overview
EDTA
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decreases enzyme thermal stability
N,N,N',N'-tetramethyl-4-phenylenediamine
i.e. Wurster's blue
phenazine ethosulfate
the articficial cofactor exhibits strong substrate inhibition
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cyanide
suppresses the peculiar endogenous reaction of methanol dehydrogenase, and is also both an activator of substrate-dependent activity and a competitive inhibitor with respect to methanol, the two activities correspond to two distinct binding sites for cyanide, overview
NH4+
obligatory activator
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91.4
butanol
pH 9.0, 30°C, assayed with N,N,N',N'-tetramethyl-4-phenylenediamine
3.39
ethanol
pH 9.0, 30°C, assayed with N,N,N',N'-tetramethyl-4-phenylenediamine
0.56
methanol
pH 9.0, 30°C, assayed with N,N,N',N'-tetramethyl-4-phenylenediamine
3.22
N,N,N',N'-tetramethyl-4-phenylenediamine
pH 9.0 30°C
11.8
phenazine ethosulfate
pH 9.0, 30°C
10.7
Propanol
pH 9.0, 30°C, assayed with N,N,N',N'-tetramethyl-4-phenylenediamine
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9.37
N,N,N',N'-tetramethyl-4-phenylenediamine
pH 9.0 30°C
0.59
phenazine ethosulfate
pH 9.0, 30°C
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9
assay at
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30
-
assay at
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P12293 (large subunit, alpha) and P12293 (small subunit, beta)
UniProt
brenda
strain ATCC 13543
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brenda
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brenda
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brenda
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DHM1_PARDE
631
1
69799
Swiss-Prot
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12000
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x * 67000 + x * 12000, SDS-PAGE
67000
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x * 67000 + x * 12000, SDS-PAGE
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?
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x * 67000 + x * 12000, SDS-PAGE
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purified enzyme, hanging drop vapor diffusion and macro-seeding, mixing of protein solution containing 5 mg/ml protein, 0.1 M Tris-HCl, pH 8.3, 0.2 M Li2SO4, 30% PEG 3350, with precipitant solution containing 0.1 M Tris-HCl, pH 8.5, 30% PEG 4000, 0.2 M Li2SO4, several days, X-ray diffraction structure determination and analysis at 2.5 A resolution, modelling
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4.5 - 9
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30°C, 20 h, stable below pH 9, rapid loss of activity above pH 9
686814
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10 - 60
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10 min, the purified enzyme is quite stable within this range, significant loss of activity occurs at higher temperatures, Ca2+ enhances the thermal stability, while EDTA reduces it
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native enzyme 6.8fold from periplasm to homogeneity by ultrafiltration, dialysis, anion exchange chromatography, and gel filtration
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Harris, T.K.; Davidson, V.L.
A new kinetic model for the steady-state reactions of the quinoprotein methanol dehydrogenase from Paracoccus denitrificans
Biochemistry
32
4362-4368
1993
Paracoccus denitrificans (P12293)
brenda
Davidson, V.L.; Wu, J.; Miller, B.; Jones, L.H.
Factors affecting the stability of methanol dehydrogenase from Paracoccus denitrificans
FEMS Microbiol. Lett.
94
53-58
1992
Paracoccus denitrificans
brenda
Xia, Z.X.; Dai, W.W.; He, Y.N.; White, S.A.; Mathews, F.S.; Davidson, V.L.
X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i
J. Biol. Inorg. Chem.
8
843-854
2003
Paracoccus denitrificans (P12293), Paracoccus denitrificans
brenda
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1.1.2.B2 quinoprotein methanol dehydrogenase (cytochrome c551i)
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