PROSITE documentation PDOC50980

Acetyl-coenzyme A carboxyltransferase domain profiles




Description

Acetyl-coenzyme A carboxylase (EC 6.4.1.2) (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>) [3]. 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:

  • Methylcrotonyl-CoA carboxylase β chain, mitochondrial precursor (EC 6.4.1.4).
  • Glutaconyl-CoA decarboxylase α subunit (EC 4.1.1.70).
  • Propionyl-CoA carboxylase β chain (EC 6.4.1.3) (PCCase).

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

COA_CT_CTER, PS50989; Acetyl-coenzyme A (CoA) carboxyltransferase C-terminal domain profile  (MATRIX)

COA_CT_NTER, PS50980; Acetyl-coenzyme A (CoA) carboxyltransferase N-terminal domain profile  (MATRIX)


References

1AuthorsKnowles J.R.
TitleThe mechanism of biotin-dependent enzymes.
SourceAnnu. Rev. Biochem. 58:195-221(1989).
PubMed ID2673009
DOI10.1146/annurev.bi.58.070189.001211;

2AuthorsAttwood P.V., Wallace J.C.
TitleChemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes.
SourceAcc. Chem. Res. 35:113-120(2002).
PubMed ID11851389

3AuthorsZhang H., Yang Z., Shen Y., Tong L.
TitleCrystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.
SourceScience 299:2064-2067(2003).
PubMed ID12663926
DOI10.1126/science.1081366



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