Evidence that the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium.
When 7-mercaptoheptanoylthreonine phosphate (HS-HTP) was used as the sole source of electrons for reductive demethylation of 2-(methylthio)-ethanesulfonic acid (CH3-S-CoM) by cell extracts of Methanobacterium thermoautotrophicum strain delta H, the heterodisulfide of coenzyme M and HS-HTP (CoM-S-S-HTP) was quantitatively produced: HS-HTP + CH3-S-CoM----CH4 + CoM-S-S-HTP. CH4 and CoM-S-S-HTP were produced stoichiometrically in a ratio of 1:1. Coenzyme M (HS-CoM) inhibited HS-HTP driven methanogenesis indicating that CH3-S-CoM rather than HS-CoM was the substrate for CoM-S-S-HTP formation.
D019605:Euryarchaeota / Q000378:metabolism*; D008623:Mercaptoethanol / Q000031:analogs & derivatives*; D015080:Mesna / Q000378:metabolism*; D008697:Methane / Q000378:metabolism; D010084:Oxidation-Reduction; D010769:Phosphothreonine / Q000031:analogs & derivatives* / Q000378:metabolism; D013440:Sulfides / Q000378:metabolism; D013912:Threonine / Q000031:analogs & derivatives*
D013440:Sulfides; C049349:7-mercaptoheptanoylthreonine phosphate; D010769:Phosphothreonine; D013912:Threonine; D008623:Mercaptoethanol; D015080:Mesna; D008697:Methane