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Information on EC 1.1.2.B2 - quinoprotein methanol dehydrogenase (cytochrome c551i) and Organism(s) Paracoccus denitrificans and UniProt Accession P12293

for references in articles please use BRENDA:EC1.1.2.B2
preliminary BRENDA-supplied EC number
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Paracoccus denitrificans
UNIPROT: P12293 not found.
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The taxonomic range for the selected organisms is: Paracoccus denitrificans
The expected taxonomic range for this enzyme is: Paracoccus denitrificans
Synonyms
MEDH, MEDH-PD, methanol dehydrogenase, quinoprotein methanol dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methanol dehydrogenase
-
quinoprotein methanol dehydrogenase
-
methanol dehydrogenase
-
-
SYSTEMATIC NAME
IUBMB Comments
methanol:ferricytochrome c551i oxidoreductase
-
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
-
-
-
?
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 + 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
-
-
-
?
methanol + nitroblue tetrazolium
formaldehyde + reduced nitroblue tetrazolium
show the reaction diagram
-
-
-
-
?
additional information
?
-
interaction of the enzyme with cytochrome c551i, and electron transfer from reduced pyrroloquinoline quinone to the cytochrome, interface structure, modelling, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
pyrroloquinoline quinone
-
non-covalently bound
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
increases enzyme thermal stability, Ca2+ has a structural role
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
N,N,N',N'-tetramethyl-4-phenylenediamine
i.e. Wurster's blue
phenazine ethosulfate
the articficial cofactor exhibits strong substrate inhibition
EDTA
-
decreases enzyme thermal stability
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
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
pH 9.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.4
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P12293 (large subunit, alpha) and P12293 (small subunit, beta)
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DHM1_PARDE
631
1
69799
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
-
x * 67000 + x * 12000, SDS-PAGE
67000
-
x * 67000 + x * 12000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9
-
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
-
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team