KEGG   ENZYME: 1.1.2.7Help
Entry
EC 1.1.2.7                  Enzyme                                 

Name
methanol dehydrogenase (cytochrome c);
methanol dehydrogenase;
MDH
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With a cytochrome as acceptor
BRITE hierarchy
Sysname
methanol:cytochrome c oxidoreductase
Reaction(IUBMB)
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ [RN:R10713]
Reaction(KEGG)
Substrate
primary alcohol [CPD:C00226];
ferricytochrome cL [CPD:C18233]
Product
aldehyde [CPD:C00071];
ferrocytochrome cL [CPD:C18234];
H+ [CPD:C00080]
Comment
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).
History
EC 1.1.2.7 created 1972 as EC 1.1.99.8, modified 1982, part transferred 2010 to EC 1.1.2.7
Pathway
ec00010  Glycolysis / Gluconeogenesis
ec00625  Chloroalkane and chloroalkene degradation
ec00680  Methane metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
ec01130  Biosynthesis of antibiotics
Orthology
K14028  methanol dehydrogenase (cytochrome c) subunit 1
K14029  methanol dehydrogenase (cytochrome c) subunit 2
Genes
DKO: I596_1064 I596_1067
MCA: MCA0779(mxaF) MCA0782(mxaI)
MMT: Metme_4317 Metme_4320
MDN: JT25_020965 JT25_020980
MDH: AYM39_15600 AYM39_15615
MKO: MKLM6_3207 MKLM6_3210
MAH: MEALZ_3445(mxaI) MEALZ_3448(mxaF)
MPSY: CEK71_12435 CEK71_12450
MEJ: Q7A_534 Q7A_537
MEC: Q7C_2122 Q7C_2125
MEA: Mex_1p4535(mxaI) Mex_1p4538(mxaF)
MDI: METDI5141(mxaI) METDI5145(mxaF)
MOR: MOC_4859 MOC_4862(mxaF)
MAQU: Maq22A_1p33165(mxaF) Maq22A_1p33180(mxaI)
HMC: HYPMC_0485(mxaF) HYPMC_0488(mxaI)
FIL: BN1229_v1_2515(mxaF) BN1229_v1_2518(mxaI)
FIY: BN1229_v1_3398(mxaI) BN1229_v1_3401(mxaF)
MSC: BN69_2570(mxaF) BN69_2573
ALI: AZOLI_p10948(moxF1) AZOLI_p10951(moxI)
MIN: Minf_0992(gcd)
MOX: DAMO_0112(mxaF) DAMO_0115(mxaI)
 » show all
Taxonomy
Reference
1  [PMID:4378696]
  Authors
Anthony C, Zatman LJ
  Title
The microbial oxidation of methanol. 2. The methanol-oxidizing enzyme of Pseudomonas sp. M 27.
  Journal
Biochem J 92:614-21 (1964)
Reference
2  [PMID:6049934]
  Authors
Anthony C, Zatman LJ
  Title
The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group.
  Journal
Biochem J 104:960-9 (1967)
Reference
3  [PMID:6250827]
  Authors
Duine JA, Frank J, Verwiel PE.
  Title
Structure and activity of the prosthetic group of methanol dehydrogenase.
  Journal
Eur J Biochem 108:187-92 (1980)
DOI:10.1111/j.1432-1033.1980.tb04711.x
Reference
4  [PMID:471057]
  Authors
Salisbury SA, Forrest HS, Cruse WB, Kennard O.
  Title
A novel coenzyme from bacterial primary alcohol dehydrogenases.
  Journal
Nature 280:843-4 (1979)
Reference
5  [PMID:1311606]
  Authors
Cox JM, Day DJ, Anthony C
  Title
The interaction of methanol dehydrogenase and its electron acceptor, cytochrome cL in methylotrophic bacteria.
  Journal
Biochim Biophys Acta 1119:97-106 (1992)
DOI:10.1016/0167-4838(92)90240-E
  Sequence
Reference
6  [PMID:7656012]
  Authors
Blake CC, Ghosh M, Harlos K, Avezoux A, Anthony C
  Title
The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues.
  Journal
Nat Struct Biol 1:102-5 (1994)
  Sequence
Reference
7  [PMID:9930981]
  Authors
Xia ZX, He YN, Dai WW, White SA, Boyd GD, Mathews FS
  Title
Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 A resolution.
  Journal
Biochemistry 38:1214-20 (1999)
DOI:10.1021/bi9822574
Reference
8  [PMID:11502173]
  Authors
Afolabi PR, Mohammed F, Amaratunga K, Majekodunmi O, Dales SL, Gill R, Thompson D, Cooper JB, Wood SP, Goodwin PM, Anthony C
  Title
Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L).
  Journal
Biochemistry 40:9799-809 (2001)
DOI:10.1021/bi002932l
  Sequence
Reference
9  [PMID:12686102]
  Authors
Anthony C, Williams P
  Title
The structure and mechanism of methanol dehydrogenase.
  Journal
Biochim Biophys Acta 1647:18-23 (2003)
DOI:10.1016/S1570-9639(03)00042-6
Reference
10 [PMID:15608378]
  Authors
Williams PA, Coates L, Mohammed F, Gill R, Erskine PT, Coker A, Wood SP, Anthony C, Cooper JB
  Title
The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens.
  Journal
Acta Crystallogr D Biol Crystallogr 61:75-9 (2005)
DOI:10.1107/S0907444904026964
Other DBs
ExplorEnz - The Enzyme Database: 1.1.2.7
IUBMB Enzyme Nomenclature: 1.1.2.7
ExPASy - ENZYME nomenclature database: 1.1.2.7
UM-BBD (Biocatalysis/Biodegradation Database): 1.1.2.7
BRENDA, the Enzyme Database: 1.1.2.7
CAS: 37205-43-9

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