Information on EC 1.1.2.B2 - quinoprotein methanol dehydrogenase (cytochrome c551i)

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The expected taxonomic range for this enzyme is: Paracoccus denitrificans

EC NUMBER
COMMENTARY hide
1.1.2.B2
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
quinoprotein methanol dehydrogenase (cytochrome c551i)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
methanol + 2 ferricytochrome c551i = formaldehyde + 2 ferrocytochrome c551i + 2 H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
methanol:ferricytochrome c551i oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
butanol + N,N,N',N'-tetramethyl-4-phenylenediamine
butyraldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
show the reaction diagram
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?
ethanol + N,N,N',N'-tetramethyl-4-phenylenediamine
acetaldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
show the reaction diagram
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-
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?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
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methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
show the reaction diagram
methanol + N,N,N',N'-tetramethyl-4-phenylenediamine
formaldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
show the reaction diagram
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?
methanol + nitroblue tetrazolium
formaldehyde + reduced nitroblue tetrazolium
show the reaction diagram
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?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
show the reaction diagram
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
show the reaction diagram
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyrroloquinoline quinone
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
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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
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i.e. Wurster's blue
phenazine ethosulfate
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the articficial cofactor exhibits strong substrate inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
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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+
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obligatory activator
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
91.4
butanol
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pH 9.0, 30°C, assayed with N,N,N',N'-tetramethyl-4-phenylenediamine
3.39
ethanol
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pH 9.0, 30°C, assayed with N,N,N',N'-tetramethyl-4-phenylenediamine
0.56
methanol
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pH 9.0, 30°C, assayed with N,N,N',N'-tetramethyl-4-phenylenediamine
3.22
N,N,N',N'-tetramethyl-4-phenylenediamine
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pH 9.0 30°C
11.8
phenazine ethosulfate
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pH 9.0, 30°C
10.7
Propanol
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pH 9.0, 30°C, assayed with N,N,N',N'-tetramethyl-4-phenylenediamine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.37
N,N,N',N'-tetramethyl-4-phenylenediamine
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pH 9.0 30°C
0.59
phenazine ethosulfate
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pH 9.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.4
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
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x * 67000 + x * 12000, SDS-PAGE
67000
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x * 67000 + x * 12000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 67000 + x * 12000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9
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30°C, 20 h, stable below pH 9, rapid loss of activity above pH 9
686814
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 6.8fold from periplasm to homogeneity by ultrafiltration, dialysis, anion exchange chromatography, and gel filtration
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