CO-methylating acetyl-CoA synthase
From Wikipedia, the free encyclopedia
In enzymology, a CO-methylating acetyl-CoA synthase (EC 2.3.1.169) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + corrinoid protein
CO + methylcorrinoid protein + CoA
Thus, the two substrates of this enzyme are acetyl-CoA and corrinoid protein, whereas its 3 products are CO, methylcorrinoid protein, and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:corrinoid protein O-acetyltransferase.
[edit] References
- IUBMB entry for 2.3.1.169
- BRENDA references for 2.3.1.169 (Recommended.)
- PubMed references for 2.3.1.169
- PubMed Central references for 2.3.1.169
- Google Scholar references for 2.3.1.169
- Ragsdale SW, Wood HG (1985). "Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis". J. Biol. Chem. 260: 3970–7. PMID 2984190.
- Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL (2002). "A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase". Science. 298: 567–72. doi:. PMID 12386327.

