7-Mercaptoheptanoylthreonine phosphate functions as component B in ATP-independent methane formation from methyl-CoM with reduced cobalamin as electron donor.
Purified methyl-CoM reductase of Methanobacterium thermoautotrophicum (strain Marburg) catalyzed the reduction of methyl-CoM to methane with reduced cobalamin, when either synthetic 7-mercaptoheptanoylthreonine phosphate (HS-HTP) or naturally occurring component B was present. With both compounds the same maximal specific activity was obtained and ATP was neither required nor stimulatory. These findings indicate that HS-HTP functions as component B and do not support the idea that HS-HT is only active in an adenosine monophosphorylated form.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D019605:Euryarchaeota; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D008623:Mercaptoethanol / Q000031:analogs & derivatives*; D015080:Mesna / Q000031:analogs & derivatives* / Q000378:metabolism; D008697:Methane / Q000378:metabolism*; D010769:Phosphothreonine / Q000031:analogs & derivatives* / Q000378:metabolism; D013912:Threonine / Q000031:analogs & derivatives*; D014805:Vitamin B 12 / Q000378:metabolism*
C049349:7-mercaptoheptanoylthreonine phosphate; D010769:Phosphothreonine; D013912:Threonine; C023349:methyl coenzyme M; D008623:Mercaptoethanol; D000255:Adenosine Triphosphate; D008274:Magnesium; D015080:Mesna; D008697:Methane; D014805:Vitamin B 12