| Entry |
|
|---|
| Name |
coenzyme-B sulfoethylthiotransferase;
methyl-CoM reductase;
methyl coenzyme M reductase |
|---|
| Class |
Transferases;
Transferring sulfur-containing groups;
Transferring alkylthio groups
 |
|---|
| Sysname |
2-(methylthio)ethanesulfonate:N-(7-thioheptanoyl)-3-O-phosphothreoni
ne S-(2-sulfoethyl)thiotransferase |
|---|
| Reaction(IUBMB) |
2-(methylthio)ethanesulfonate (methyl-CoM) +
N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) =
CoM-S-S-CoB + methane [RN:R04541] |
|---|
| Reaction(KEGG) |
R04541
 |
|---|
| Substrate |
2-(methylthio)ethanesulfonate [CPD:C03920];
N-(7-mercaptoheptanoyl)threonine 3-O-phosphate [CPD:C04628] |
|---|
| Product |
CoM-S-S-CoB [CPD:C04832];
methane [CPD:C01438] |
|---|
| Comment |
The enzyme from methanogenic bacteria requires the hydroporphinoid
nickel complex coenzyme F430. Highly specific for coenzyme B with a
heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor
substrates. The sulfide sulfur can be replaced by selenium but not
by oxygen. |
|---|
| Pathway |
PATH: ec00790 Folate biosynthesis
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00399 methyl-coenzyme M reductase alpha subunit
KO: K00401 methyl-coenzyme M reductase beta subunit
KO: K00402 methyl-coenzyme M reductase gamma subunit |
|---|
| Genes |
MJA: MJ0081 MJ0082 MJ0083 MJ0842 MJ0845 MJ0846
MFE: Mefer_0934 Mefer_0937 Mefer_0938
MMP: MMP1555(mcrB) MMP1558(mcrG) MMP1559(mcrA)
MMQ: MmarC5_0017 MmarC5_0018 MmarC5_0021
MMX: MmarC6_1111 MmarC6_1112 MmarC6_1115
MMZ: MmarC7_0802 MmarC7_0805 MmarC7_0806
MAE: Maeo_1264 Maeo_1267 Maeo_1268
MVN: Mevan_0868 Mevan_0871 Mevan_0872
MAC: MA4546 MA4547 MA4550
MBA: Mbar_A0893 Mbar_A0894 Mbar_A0897
MMA: MM_1240 MM_1241 MM_1244
MBU: Mbur_2417 Mbur_2418 Mbur_2421
MTP: Mthe_0569 Mthe_0570 Mthe_0572
MHU: Mhun_2144 Mhun_2147 Mhun_2148
MLA: Mlab_1066 Mlab_1067 Mlab_1068 Mlab_1561 Mlab_1562 Mlab_1565
MEM: Memar_0375 Memar_0377 Memar_0378 Memar_0613 Memar_0614
Memar_0617
MBN: Mboo_0582 Mboo_0583 Mboo_0586
MPL: Mpal_2305 Mpal_2308 Mpal_2309
MTH: MTH1129 MTH1130 MTH1132 MTH1164 MTH1165 MTH1168
MST: Msp_0318(mrtB) Msp_0320(mrtG) Msp_0321(mrtA)
MSI: Msm_0902 Msm_0903 Msm_0905 Msm_1016 Msm_1019
MKA: MK0651(mcrB) MK0654(mcrG) MK0655(mcrA)
RCI: RCIX2059(mcrB) RCIX2062(mcrG) RCIX2063(mcrA)
 |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:3122735]
Bobik TA, Olson KD, Noll KM, Wolfe RS.
Evidence that the heterodisulfide of coenzyme M and
7-mercaptoheptanoylthreonine phosphate is a product of the
methylreductase reaction in Methanobacterium.
Biochem. Biophys. Res. Commun. 149 (1987) 455-60.
Methanobacterium thermoautotrophicum [GN:mth] |
|---|
Reference
Authors
Title
Journal
|
2
Ellermann, J., Hedderich, R., Boecher, R. and Thauer, R.K.
The final step in methane formation: investigations with highly
purified methyl coenzyme M reductase component C from
Methanobacterium thermoautotrophicum (strain Marburg).
Eur. J. Biochem. 184 (1988) 63-68. |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:9367957]
Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK.
Crystal structure of methyl-coenzyme M reductase: the key enzyme of
biological methane formation.
Science. 278 (1997) 1457-62.
Methanobacterium thermoautotrophicum [GN:mth] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:11072815]
Signor L, Knuppe C, Hug R, Schweizer B, Pfaltz A, Jaun B.
Methane formation by reaction of a methyl thioether with a
photo-excited nickel thiolate--a process mimicking methanogenesis in
archaea.
Chemistry. 6 (2000) 3508-16.
methanogenic archaea |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 2.8.4.1
IUBMB Enzyme Nomenclature: 2.8.4.1
ExPASy - ENZYME nomenclature database: 2.8.4.1
UM-BBD (Biocatalysis/Biodegradation Database): 2.8.4.1
BRENDA, the Enzyme Database: 2.8.4.1 |
|---|
