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PMID: 4901473 Published · ppublish English Journal Article

Acetyl CoA carboxylase, II. Deomonstration of biotin-protein and biotin carboxylase subunits.

Alberts AW, Nervi AM, Vagelos PR

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.

MeSH Terms
Bacterial Proteins Biotin Carboxy-Lyases Coenzyme A Escherichia coli/enzymology Molecular Weight Ovalbumin Protein Binding
Chemicals
Bacterial Proteins Biotin Ovalbumin Carboxy-Lyases Coenzyme A
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Alberts A W
Nervi A M
Vagelos P R
References (7)
7 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1969-08-00
Pages
1319-26
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC223467
Subset
IM
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