|PROSITE documentation PDOC50980 [for PROSITE entry PS50980]|
Acetyl-coenzyme A carboxylase (EC 22.214.171.124) (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 perform the second part of the reaction [1,2].
The N- and C-terminal regions of the carboxyltransferase domain share similar polypeptide backbone folds, with a central β-β-α superhelix (see <PDB:1OD2>) . 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.
The acetyl-coenzyme A carboxyltransferase domain is also found in the following enzymes:
We developed two profiles for this domain, one that spans the N subdomain and also recognizes the bacterial ACC β-subunit, the other profile is directed against the C subdomain and recognizes also the α-subunit of bacterial ACC.Note:
Herbicide that target the carboxyltransferase domain are powerful inhibitors of plastid ACC and can kill sensitive plants by shutting down fatty acid biosynthesis.Last update:
August 2016 / Profiles revised.
PROSITE methods (with tools and information) covered by this documentation:
|Title||The mechanism of biotin-dependent enzymes.|
|Source||Annu. Rev. Biochem. 58:195-221(1989).|
|2||Authors||Attwood P.V., Wallace J.C.|
|Title||Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes.|
|Source||Acc. Chem. Res. 35:113-120(2002).|
|3||Authors||Zhang H., Yang Z., Shen Y., Tong L.|
|Title||Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.|