| Literature DB >> 4901473 |
A W Alberts, A M Nervi, P R Vagelos.
Abstract
Previous work has shown that Escherichia coli acetyl CoA carboxylase is composed of two dissimilar protein components, E(a) which contains covalently bound biotin and forms E(a)-CO(2)-from HCO(3)- and ATP, and E(b) which is involved in the transfer of the carboxyl group from E(a)-CO(2)- to acetyl CoA, forming malonyl CoA. E(a) 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.Entities:
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Year: 1969 PMID: 4901473 PMCID: PMC223467 DOI: 10.1073/pnas.63.4.1319
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205