Enzyme

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     2. Transferases
        2.8 Transferring sulfur-containing groups
            2.8.4 Transferring alkylthio groups
ID:2.8.4.1
Description:Coenzyme-B sulfoethylthiotransferase.
Alternative Name: Methyl-CoM reductase.
Methyl coenzyme M reductase.
Cath: 3.30.70.470; 3.90.320.20; 3.90.390.10; 1.20.840.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.8.4.1
BRENDA Enzyme Link: BRENDA 2.8.4.1
KEGG Enzyme Link: KEGG2.8.4.1
BioCyc Enzyme Link: BioCyc 2.8.4.1
ExPASy Enzyme Link: ExPASy2.8.4.1
EC2PDB Enzyme Link: EC2PDB 2.8.4.1
ExplorEnz Enzyme Link: ExplorEnz 2.8.4.1
PRIAM enzyme-specific profiles Link: PRIAM 2.8.4.1
IntEnz Enzyme Link: IntEnz 2.8.4.1
MEDLINE Enzyme Link: MEDLINE 2.8.4.1
MSA:

2.8.4.1;

Phylogenetic Tree:

2.8.4.1;

Uniprot:
M-CSA:
RHEA:12532 coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methane
RULE(radius=1) [*:1]-[S;H0;+0:2]-[CH3;+0:3].[*:4]-[SH;+0:5]>>[*:4]-[S;H0;+0:5]-[S;H0;+0:2]-[*:1].[CH4;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK1997 Nov 219367957
Properties of the two isoenzymes of methyl-coenzyme M reductase in Methanobacterium thermoautotrophicum.Bonacker LG, Baudner S, Mörschel E, Böcher R, Thauer RK1993 Oct 158223602
Intermediates in the catalytic cycle of methyl coenzyme M reductase: isotope exchange is consistent with formation of a σ-alkane-nickel complex.Scheller S, Goenrich M, Mayr S, Thauer RK, Jaun B2010 Oct 2520857468
Binding of coenzyme B induces a major conformational change in the active site of methyl-coenzyme M reductase.Ebner S, Jaun B, Goenrich M, Thauer RK, Harmer J2010 Jan 2020014831
Geometric and electronic structures of the Ni(I) and methyl-Ni(III) intermediates of methyl-coenzyme M reductase.Sarangi R, Dey M, Ragsdale SW2009 Apr 1419243132
Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase.Hinderberger D, Ebner S, Mayr S, Jaun B, Reiher M, Goenrich M, Thauer RK, Harmer J2008 Nov18712421
Characterization of alkyl-nickel adducts generated by reaction of methyl-coenzyme m reductase with brominated acids.Dey M, Kunz RC, Lyons DM, Ragsdale SW2007 Oct 2317902704
Post-translational modifications in the active site region of methyl-coenzyme M reductase from methanogenic and methanotrophic archaea.Kahnt J, Buchenau B, Mahlert F, Krüger M, Shima S, Thauer RK2007 Sep17725644
Spectroscopic and kinetic studies of the reaction of bromopropanesulfonate with methyl-coenzyme M reductase.Kunz RC, Horng YC, Ragsdale SW2006 Nov 1016966321
Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate--a process mimicking methanogenesis in archaea.Signor L, Knuppe C, Hug R, Schweizer B, Pfaltz A, Jaun B2000 Oct 211072815