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

for references in articles please use BRENDA:EC1.1.2.B2
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The expected taxonomic range for this enzyme is: Paracoccus denitrificans

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EC NUMBER
COMMENTARY hide
1.1.2.B2
preliminary BRENDA-supplied EC number
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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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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
methanol:ferricytochrome c551i oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
-
-
-
?
ethanol + N,N,N',N'-tetramethyl-4-phenylenediamine
acetaldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
show the reaction diagram
-
-
-
?
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
-
-
-
?
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
-
-
?
propanol + N,N,N',N'-tetramethyl-4-phenylenediamine
propionaldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
show the reaction diagram
-
-
-
?
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyrroloquinoline quinone
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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
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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+
-
obligatory activator
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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
-
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
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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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.37
N,N,N',N'-tetramethyl-4-phenylenediamine
-
pH 9.0 30°C
0.59
phenazine ethosulfate
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pH 9.0, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.4
-
purified enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 67000 + x * 12000, SDS-PAGE
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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
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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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.2.B2)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)