Any feedback?
Information on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c) and Organism(s) Methylophilus methylotrophus and UniProt Accession P38539
for references in articles please use BRENDA:EC1.1.2.7Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.1.2.7 methanol dehydrogenase (cytochrome c)IUBMB Comments
A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria. It uses the novel specific cytochrome cL as acceptor. Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde. Activity is stimulated by ammonia or methylamine. It is usually assayed with phenazine methosulfate. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ. It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function).
Specify your search results
Word Map
- 1.1.2.7
-
1.1.99.8
- phenazine
- methylamine
- formaldehyde
- hyphomicrobium
-
quinoproteins
-
pyrroloquinoline
- methylophilus
- denitrificans
-
paracoccus
- methylotrophus
-
half-reaction
-
linewidth
-
quinone-dependent
-
methylobacterium
-
protiated
-
wurster
-
methylomonas
-
one-electron
- extorquens
The taxonomic range for the selected organisms is: Methylophilus methylotrophus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
type i mdh, hd-mdh, pqq-dependent methanol dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MDH
methanol dehydrogenase
quinoprotein methanol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
chemical structure of pyrroloquinoline quinone and hydride transfer mechanism of the enzymatic reaction catalyzed by MEDH, overview
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
additionelimination mechanism and hydride transfer mechanism, the catalytic mechanism, with a tetrahedral intermediate, involves the quinone containing prosthetic group, substrate binding and active site structures, overview, the oxygen atoms of the PQQ are involved in several hydrogen bonds with the residues Glu55, Arg109, Thr153, Ser168, Arg324 and Asn387
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
detailed mechanism of methanol oxidation involving residues Asp297 and Glu171, structure-activity analysis by quantum mechanics and molecular mechanics, QM/MM, selfconsistent-charge density-functional tight-binding, SCC-DFTB, and molecular dynamics, the transition state involves Glu171-CO2- as general base
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
methanol:cytochrome c oxidoreductase
A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria. It uses the novel specific cytochrome cL as acceptor. Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde. Activity is stimulated by ammonia or methylamine. It is usually assayed with phenazine methosulfate. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ. It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function).
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
additional information
?
-
oxidation of alcohols by direct hydride transfer to the pyrroloquinoline quinone cofactor, catalytic mechanism, ping-pong kinetic schemes, and transition state structures, analysis by ab initio quantum mechanical methods, hydride transfer from the Calpha-position of the substrate alcohol or aldehyde directly to the C-5 carbon of PQQ is energetically feasible, detailed overview
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
2,7,9-tricarboxypyrroloquinoline quinone
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
pyrroloquinoline quinone
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
pyrroloquinoline quinone
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
pyrroloquinoline quinone
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
pyrroloquinoline quinone
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
pyrroloquinoline quinone
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
two Ca2+ ions per enzyme tetramer, essential for the enzymatic activity
Ca2+
Ca2+
-
required for catalytic activity, binding structure, overview
Ca2+
required for activity, functional role analysis, overview
Ca2+
-
active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
thermodynamics
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, which catalyzes the oxidation of methanol to formaldehyde, active site structure with pyrroloquinoline quinone and Ca2+, substrate binding structure, overview
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62000
-
2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination
8000
-
2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits
tetramer
additional information
tetramer
-
2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination
additional information
three-dimensional structrue determination of MEDH with bound methanol or ethanol, overview
additional information
-
the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme, 5 mg/mL protein in 50 mM Tris-HCl, pH 8.25, and 13.5% PEG 8000, mixed with crystallization solution containing 1 and 50 mM methanol resulting in crystal forms A, B or C with or without incorporated methanol or ethanool, 20°C, X--ray diffraction structure determination and analysis at 1.5-3.0 A resolution, molecular modeling
X-ray diffraction strcuture determination and analysis at 2.6 A resolution, multiple isomorphous replacement, modelling
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leopoldini, M.; Russo, N.; Toscano, M.
The preferred reaction path for the oxidation of methanol by PQQ-containing methanol dehydrogenase: addition-elimination versus hydride-transfer mechanism
Chem. Eur. J.
13
2109-2117
2007
Methylophilus methylotrophus, Methylophilus methylotrophus W3A1
Zhang, X.; Reddy, S.Y.; Bruice, T.C.
Mechanism of methanol oxidation by quinoprotein methanol dehydrogenase
Proc. Natl. Acad. Sci. USA
104
745-749
2007
Methylophilus methylotrophus (P38539 and P38540)
Xia, Z.X.; Dai, W.W.; Xiong, J.P.; Hao, Z.P.; Davidson, V.L.; White, S.; Mathews, F.S.
The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution
J. Biol. Chem.
267
22289-22297
1992
Methylophilus methylotrophus (P38539 and P38540), Methylophilus methylotrophus W3A1 (P38539 and P38540)
Jongejan, A.; Jongejan, J.A.; Hagen, W.R.
Direct hydride transfer in the reaction mechanism of quinoprotein alcohol dehydrogenases: a quantum mechanical investigation
J. Comput. Chem.
22
1732-1749
2001
Methylorubrum extorquens (P16027 and P14775), Methylophilus methylotrophus (P38539 and P38540)
Zheng, Y.J.; Bruice, T.C.
Conformation of coenzyme pyrroloquinoline quinone and role of Ca2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase
Proc. Natl. Acad. Sci. USA
94
11881-11886
1997
Methylophilus methylotrophus (P38539 and P38540), Methylophilus methylotrophus W3A1 (P38539 and P38540)
Zheng, Y.J.; Xia Zx, Y.J.; Chen Zw, Y.J.; Mathews, F.S.; Bruice, T.C.
Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation
Proc. Natl. Acad. Sci. USA
98
432-434
2001
Methylophilus methylotrophus (P38539 and P38540), Methylophilus methylotrophus W3A1 (P38539 and P38540)
Li, J.; Gan, J.H.; Mathews, F.S.; Xia, Z.X.
The enzymatic reaction-induced configuration change of the prosthetic group PQQ of methanol dehydrogenase
Biochem. Biophys. Res. Commun.
406
621-626
2011
Methylophilus methylotrophus (P38539), Methylophilus methylotrophus W3A1 (P38539)
Gvozdev, A.; Tukhvatullin, I.; Gvozdev, R.
Quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases
Biochemistry
77
843-856
2012
Diplococcus sp., Methylophilus methylotrophus, Methylophilus methylotrophus W3A1, Methylorubrum extorquens, Paracoccus denitrificans, Paracoccus pantotrophus, Pseudomonas sp., Rhodoblastus acidophilus
EXTERNAL LINKS (specific for EC-Number 1.1.2.7)
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)
Legal
Curated at
Member of
