Any feedback?
No. of entries
Information on EC 1.1.2.B2 - quinoprotein methanol dehydrogenase (cytochrome c551i)
for references in articles please use BRENDA:EC1.1.2.B2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.2 With a cytochrome as acceptor
1.1.2.B2 quinoprotein methanol dehydrogenase (cytochrome c551i)
The expected taxonomic range for this enzyme is: Paracoccus denitrificans
Reaction Schemes
showSynonyms
MEDH, MEDH-PD, methanol dehydrogenase, quinoprotein methanol dehydrogenase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
methanol dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
methanol + 2 ferricytochrome c551i = formaldehyde + 2 ferrocytochrome c551i + 2 H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
methanol:ferricytochrome c551i oxidoreductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
butanol + N,N,N',N'-tetramethyl-4-phenylenediamine
butyraldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
Substrates: -
Products: -
Products: -
?
ethanol + N,N,N',N'-tetramethyl-4-phenylenediamine
acetaldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
Substrates: -
Products: -
Products: -
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
methanol + N,N,N',N'-tetramethyl-4-phenylenediamine
formaldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
Substrates: -
Products: -
Products: -
?
methanol + nitroblue tetrazolium
formaldehyde + reduced nitroblue tetrazolium
-
Substrates: -
Products: -
Products: -
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
Substrates: phenazine ethosulfate is a two-electron acceptor
Products: -
Products: -
?
propanol + N,N,N',N'-tetramethyl-4-phenylenediamine
propionaldehyde + reduced N,N,N',N'-tetramethyl-4-phenylenediamine
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: interaction of the enzyme with cytochrome c551i, and electron transfer from reduced pyrroloquinoline quinone to the cytochrome, interface structure, modelling, overview
Products: -
Products: -
?
methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
Substrates: -
Products: -
Products: -
?
methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
Substrates: the primary electron acceptor of MEDH-PD is cytochrome c-551i
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
Substrates: -
Products: -
Products: -
?
methanol + ferricytochrome c551i
formaldehyde + ferrocytochrome c551i
Substrates: the primary electron acceptor of MEDH-PD is cytochrome c-551i
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
increases enzyme thermal stability, Ca2+ has a structural role
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
phenazine ethosulfate
the articficial cofactor exhibits strong substrate inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
10.7
Propanol
pH 9.0, 30°C, assayed with N,N,N',N'-tetramethyl-4-phenylenediamine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P12293 (large subunit, alpha) and P12293 (small subunit, beta)
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9
-
30°C, 20 h, stable below pH 9, rapid loss of activity above pH 9
686814
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 6.8fold from periplasm to homogeneity by ultrafiltration, dialysis, anion exchange chromatography, and gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
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)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.2.B2)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
