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. 1971 Jun;68(6):1259–1263. doi: 10.1073/pnas.68.6.1259

Acetyl CoA Carboxylase: The Purified Transcarboxylase Component

Alfred W Alberts 1, Stuart G Gordon 1, P Roy Vagelos 1
PMCID: PMC389167  PMID: 4942182

Abstract

Acetyl CoA carboxylase of Escherichia coli has been resolved into three functionally dissimilar proteins: (1) biotin-carboxyl carrier protein (BCCP); (2) a biotin carboxylase component that catalyzes the Mn-ATP-dependent carboxylation of BCCP to form CO2--BCCP; and (3) a transcarboxylase component that catalyzes the transfer of the carboxyl group from CO2--BCCP to acetyl CoA to form malonyl CoA.

The transcarboxylase has been purified 1700-fold. Evidence that this protein catalyzes the transcarboxylase step includes the demonstration that it (a) catalyzes the carboxylation of BCCP, (b) catalyzes the BCCP-dependent exchange between [14C]acetyl CoA and malonyl CoA, (c) binds labeled acetyl CoA and malonyl CoA, and (d) catalyzes the decarboxylation of CO2--BCCP. On the basis of this evidence, it is concluded that the transcarboxylase component contains sites for the acyl CoA group and for biotin, the covalently bound prosthetic group of BCCP.

Keywords: acyl CoA binding, carboxylation, exchange reactions, biotin

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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