KEGG ENZYME: 1.1.2.7

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)

R10713 > R01146 R09127 R09128

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

DKO:	I596_1064 I596_1067

MCA:	MCA0779(mxaF) MCA0782(mxaI)

METU:

GNH96_04380 GNH96_04395

MMEO:

OOT43_06915 OOT43_06930

MMT:	Metme_4317 Metme_4320

MDN:	JT25_020965 JT25_020980

MDH:	AYM39_15600 AYM39_15615

MKO:	MKLM6_3207 MKLM6_3210

METL:

U737_12035 U737_12050

MPAD:

KEF85_12450 KEF85_12465

MELL:

IVG45_11190 IVG45_11205

MRP:	NM686_017355 NM686_017370

MMOT:

QZJ86_07495 QZJ86_07510

MAH:	MEALZ_3445(mxaI) MEALZ_3448(mxaF)

MBUR:

EQU24_18130 EQU24_18145

MPSY:

CEK71_12435 CEK71_12450

MMAI:

sS8_1433 sS8_1436

MSZE:

MSZNOR_0553(mxaF) MSZNOR_0556(mxaI)

MMOB:

F6R98_08155 F6R98_08170

MOZ:	MoryE10_30860 MoryE10_30890

MISZ:

MishRS11D_34140 MishRS11D_34170

MESL:

KKZ03_11810 KKZ03_11825

MEIY:

MIN45_P1622 MIN45_P1625

MCAU:

MIT9_P2079 MIT9_P2082

MEJ:	Q7A_534 Q7A_537

MEC:	Q7C_2122 Q7C_2125

MPIN:

LGT42_000430 LGT42_000445

MMAF:

GCM100_12890 GCM100_12930

MTHA:

VSX76_03530 VSX76_03545

VEI:	Veis_1826 Veis_1829

MFA:	Mfla_2041 Mfla_2044

MEI:	Msip34_0734 Msip34_0737

MEP:	MPQ_0771 MPQ_0774

MEU:	ACJ67_10795 ACJ67_10810

MPAU:

ZMTM_07630(mxaF') ZMTM_07670

BRK:	CWS35_16220 CWS35_16235

RPC:	RPC_1907 RPC_1910

RPE:	RPE_3136 RPE_3139

XDI:	EZH22_24260 EZH22_24275

SNO:	Snov_4188 Snov_4191

ANC:	GBB76_11850 GBB76_11865

APRA:

G3A50_20130 G3A50_20145

APOL:

K9D25_15345 K9D25_15360

MEA:	Mex_1p4535(mxaI) Mex_1p4538(mxaF)

MDI:	METDI5141(mxaI) METDI5145(mxaF)

MEX:	Mext_4147 Mext_4150

MCH:	Mchl_4515 Mchl_4518

MPO:	Mpop_4629 Mpop_4632

MZA:	B2G69_02645 B2G69_02660

MRD:	Mrad2831_4207 Mrad2831_4210

MNO:	Mnod_8037 Mnod_8040

MOR:	MOC_4859 MOC_4862(mxaF)

META:

Y590_20670 Y590_20685

MAQU:

Maq22A_1p33165(mxaF) Maq22A_1p33180(mxaI)

MPHY:

MCBMB27_03721 MCBMB27_03724

METD:

C0214_22745 C0214_22760

METX:

A3862_10300 A3862_10315

METS:

DK389_08295

METI:

DK427_25655 DK427_25670

MMES:

MMSR116_00880 MMSR116_00895

MIND:

mvi_06780(mxaF') mvi_06810

MOG:	MMB17_19830 MMB17_19845

MSL:	Msil_0471 Msil_0474

MTUN:

MTUNDRAET4_1609(mxaI) MTUNDRAET4_1612(mxaF)

MLG:	CWB41_12365 CWB41_12380

MEDK:

QEV83_08155 QEV83_08170

HDN:	Hden_1320 Hden_1323

HMC:	HYPMC_0485(mxaF) HYPMC_0488(mxaI)

HNI:	W911_14530 W911_14545

FIL:	BN1229_v1_2515(mxaF) BN1229_v1_2518(mxaI)

FIY:	BN1229_v1_3398(mxaI) BN1229_v1_3401(mxaF)

MCG:	GL4_0421 GL4_0424

METG:

HT051_11845 HT051_11860

MSC:	BN69_2570(mxaF) BN69_2573

MBRY:

B1812_04775

MROS:

EHO51_16425 EHO51_16440

MHEY:

H2LOC_010105 H2LOC_010120

MPAR:

F7D14_04020 F7D14_04035

MIWA:

SS37A_37970 SS37A_38000

MTW:	CQW49_14425 CQW49_14440

MECQ:

MSC49_09340 MSC49_09370(mxaF'_1)

CMET:

K6K41_19550 K6K41_19565

PLEO:

OHA_1_04073(mxaF) OHA_1_04076(mxaI)

AALA:

IGS74_17245 IGS74_17260

AALM:

LUX29_19310 LUX29_19325

AUZ:	Sa4125_26920(xoxF) Sa4125_26950

PDE:	Pden_2993 Pden_2996

PYE:	A6J80_13905 A6J80_13920

PMEH:

JWJ88_21470 JWJ88_21485

PALP:

JHW40_10385 JHW40_10400

PFEO:

E3U26_14470 E3U26_14485

GBE:	GbCGDNIH1_0344 GbCGDNIH1_0347

GBH:	GbCGDNIH2_0344 GbCGDNIH2_0347

GBC:	GbCGDNIH3_0344 GbCGDNIH3_0347

GBS:	GbCGDNIH4_0344 GbCGDNIH4_0347

ALI:	AZOLI_p10948(moxF1) AZOLI_p10951(moxI)

ATI:	AL072_18670 AL072_18685

NAO:	Y958_26250 Y958_26265

PCAY:

FRD00_19075

DPM:	FNV33_07280

SGZ:	C0216_05390

MOX:	DAMO_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

[meu:ACJ67_10795]

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

[mea:Mex_1p4538 Mex_1p4535]

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

[mea:Mex_1p4538 Mex_1p4535]

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