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. 1969 Aug;63(4):1319–1326. doi: 10.1073/pnas.63.4.1319

ACETYL COA CARBOXYLASE, II. DEMONSTRATION OF BIOTIN-PROTEIN AND BIOTIN CARBOXYLASE SUBUNITS*

Alfred W Alberts 1, A M Nervi 1,†, P R Vagelos 1
PMCID: PMC223467  PMID: 4901473

Abstract

Previous work has shown that Escherichia coli acetyl CoA carboxylase is composed of two dissimilar protein components, Ea which contains covalently bound biotin and forms Ea-CO2-from HCO3- and ATP, and Eb which is involved in the transfer of the carboxyl group from Ea-CO2- to acetyl CoA, forming malonyl CoA. Ea has been dissociated into two subunits at pH 9. One subunit, designated biotin carboxylase, catalyzes a model reaction, the ATP-dependent carboxylation of free (+)-biotin. The other subunit contains covalently bound which is carboxylated by the biotin carboxylase in the course of acetyl CoA carboxylation.

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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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