KEGG   ENZYME: 1.1.2.7
Entry
EC 1.1.2.7                  Enzyme                                 
Name
methanol dehydrogenase (cytochrome c);
methanol dehydrogenase;
MDH (ambiguous)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With a cytochrome as acceptor
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
ec00620  Pyruvate metabolism
ec00625  Chloroalkane and chloroalkene degradation
ec00680  Methane metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
Orthology
K14028  methanol dehydrogenase (cytochrome c) subunit 1
K14029  methanol dehydrogenase (cytochrome c) subunit 2
Genes
DKOI596_1064 I596_1067
MCAMCA0779(mxaF) MCA0782(mxaI)
METUGNH96_04380 GNH96_04395
MMTMetme_4317 Metme_4320
MDNJT25_020965 JT25_020980
MDHAYM39_15600 AYM39_15615
MKOMKLM6_3207 MKLM6_3210
METLU737_12035 U737_12050
MPADKEF85_12450 KEF85_12465
MELLIVG45_11190 IVG45_11205
MAHMEALZ_3445(mxaI) MEALZ_3448(mxaF)
MBUREQU24_18130 EQU24_18145
MPSYCEK71_12435 CEK71_12450
MMAIsS8_1433 sS8_1436
MMOBF6R98_08155 F6R98_08170
MOZMoryE10_30860 MoryE10_30890
MISZMishRS11D_34140 MishRS11D_34170
MESLKKZ03_11810 KKZ03_11825
MEJQ7A_534 Q7A_537
MECQ7C_2122 Q7C_2125
MPINLGT42_000430 LGT42_000445
VEIVeis_1826 Veis_1829
MFAMfla_2041 Mfla_2044
MEIMsip34_0734 Msip34_0737
MEPMPQ_0771 MPQ_0774
MEUACJ67_10795 ACJ67_10810
MPAUZMTM_07630(mxaF') ZMTM_07670
PCAYFRD00_19075
BRKCWS35_16220 CWS35_16235
RPCRPC_1907 RPC_1910
RPERPE_3136 RPE_3139
XDIEZH22_24260 EZH22_24275
SNOSnov_4188 Snov_4191
ANCGBB76_11850 GBB76_11865
APRAG3A50_20130 G3A50_20145
APOLK9D25_15345 K9D25_15360
MEAMex_1p4535(mxaI) Mex_1p4538(mxaF)
MDIMETDI5141(mxaI) METDI5145(mxaF)
MEXMext_4147 Mext_4150
MCHMchl_4515 Mchl_4518
MPOMpop_4629 Mpop_4632
MZAB2G69_02645 B2G69_02660
MRDMrad2831_4207 Mrad2831_4210
MNOMnod_8037 Mnod_8040
MORMOC_4859 MOC_4862(mxaF)
METAY590_20670 Y590_20685
MAQUMaq22A_1p33165(mxaF) Maq22A_1p33180(mxaI)
MPHYMCBMB27_03721 MCBMB27_03724
METDC0214_22745 C0214_22760
METXA3862_10300 A3862_10315
METSDK389_08295
METIDK427_25655 DK427_25670
MMESMMSR116_00880 MMSR116_00895
MINDmvi_06780(mxaF') mvi_06810
MOGMMB17_19830 MMB17_19845
MSLMsil_0471 Msil_0474
MTUNMTUNDRAET4_1609(mxaI) MTUNDRAET4_1612(mxaF)
MLGCWB41_12365 CWB41_12380
HDNHden_1320 Hden_1323
HMCHYPMC_0485(mxaF) HYPMC_0488(mxaI)
HNIW911_14530 W911_14545
FILBN1229_v1_2515(mxaF) BN1229_v1_2518(mxaI)
FIYBN1229_v1_3398(mxaI) BN1229_v1_3401(mxaF)
MCGGL4_0421 GL4_0424
METGHT051_11845 HT051_11860
MSCBN69_2570(mxaF) BN69_2573
MBRYB1812_04775
MROSEHO51_16425 EHO51_16440
MHEYH2LOC_010105 H2LOC_010120
MPARF7D14_04020 F7D14_04035
MTWCQW49_14425 CQW49_14440
CMETK6K41_19550 K6K41_19565
PLEOOHA_1_04073(mxaF) OHA_1_04076(mxaI)
AALAIGS74_17245 IGS74_17260
AALMLUX29_19310 LUX29_19325
PDEPden_2993 Pden_2996
PYEA6J80_13905 A6J80_13920
GBEGbCGDNIH1_0344 GbCGDNIH1_0347
GBHGbCGDNIH2_0344 GbCGDNIH2_0347
GBCGbCGDNIH3_0344 GbCGDNIH3_0347
GBSGbCGDNIH4_0344 GbCGDNIH4_0347
ALIAZOLI_p10948(moxF1) AZOLI_p10951(moxI)
ATIAL072_18670 AL072_18685
NAOY958_26250 Y958_26265
DPMFNV33_07280
MANYMANY_50940
SGZC0216_05390
DVCDvina_24965
MOXDAMO_0112(mxaF) DAMO_0115(mxaI)
 » show all
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)
DOI:10.1042/bj0920614
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)
DOI:10.1042/bj1040960
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)
DOI:10.1038/280843a0
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)
DOI:10.1038/nsb0294-102
  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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