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Literature summary for 2.8.4.1 extracted from

  • Wagner, T.; Kahnt, J.; Ermler, U.; Shima, S.
    Didehydroaspartate modification in methyl-coenzyme M reductase catalyzing methane formation (2016), Angew. Chem. Int. Ed. Engl., 55, 10630-10633.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methyl-CoM + CoB Methanosarcina barkeri
-
CoM-S-S-CoB + methane
-
r
methyl-CoM + CoB Methanothermobacter wolfeii
-
CoM-S-S-CoB + methane
-
r
methyl-CoM + CoB Methanothermobacter marburgensis
-
CoM-S-S-CoB + methane
-
r

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri
-
-
-
Methanothermobacter marburgensis
-
-
-
Methanothermobacter wolfeii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methyl-CoM + CoB
-
Methanosarcina barkeri CoM-S-S-CoB + methane
-
r
methyl-CoM + CoB
-
Methanothermobacter wolfeii CoM-S-S-CoB + methane
-
r
methyl-CoM + CoB
-
Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
r

Synonyms

Synonyms Comment Organism
MCR I isoform Methanosarcina barkeri
MCR I isoform Methanothermobacter wolfeii
MCR I isoform Methanothermobacter marburgensis
MCR II isoform Methanosarcina barkeri
MCR II isoform Methanothermobacter wolfeii
MCR II isoform Methanothermobacter marburgensis
methyl-coenzyme M reductase
-
Methanosarcina barkeri
methyl-coenzyme M reductase
-
Methanothermobacter wolfeii
methyl-coenzyme M reductase
-
Methanothermobacter marburgensis