v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | Acetyl-coenzyme A carboxylase ( ) (ACC), a member of the biotin-dependent enzyme family, catalyses the formation of malonyl-coenzyme A (CoA) and regulates fatty acid biosynthesis and oxidation. Biotin-dependent carboxylase enzymes perform a two step reaction: enzyme-bound biotin is first carboxylated by bicarbonate and ATP and the carboxyl group temporarily bound to biotin is subsequently transferred to an acceptor substrate such as acetyl-CoA. The carboxyltransferase domain performs the second part of the reaction [ , ].The N- and C-terminal regions of the carboxyltransferase domain share similar polypeptide backbone folds, with a central β-β-alpha superhelix [ ]. The CoA molecule is mostly associated with the N subdomain. In bacterial acetyl coenzyme A carboxylase the N and C subdomains are encoded by two different polypeptides.This entry represents the N-terminal subdomain and contains the bacterial ACC beta-subunit. |
Short Name | COA_CT_N |