Component C of the methylcoenzyme M methylreductase system contains bound 7-mercaptoheptanoylthreonine phosphate (HS-HTP).
The structure of component B of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum was recently found to be 7-mercaptoheptanoylthreonine phosphate (HS-HTP). The work described here demonstrates that this compound is found in two forms: enzyme-free and enzyme-bound. HS-HTP was found to be bound to component C of the methylcoenzyme M methylreductase system. The cofactor extracted from the protein by heat denaturation was found to comigrate with the mixed disulfide of HS-HTP and 2-mercaptoethanol by high-performance liquid chromatography, suggesting HS-HTP is not modified in the bound state.
D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D019605:Euryarchaeota / Q000201:enzymology*; D006358:Hot Temperature; D008623:Mercaptoethanol / Q000031:analogs & derivatives*; D015080:Mesna / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D011489:Protein Denaturation
D009097:Multienzyme Complexes; D008623:Mercaptoethanol; D010088:Oxidoreductases; C023895:methyl coenzyme M methylreductase; D015080:Mesna