DOI: 10.1073/pnas.68.6.1259. Acetyl CoA Carboxylase: The Purified Transcarboxylase Component

Acetyl CoA Carboxylase: The Purified Transcarboxylase Component

10.1073/pnas.68.6.1259

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

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 CO 2 - -BCCP; and ( 3 ) a transcarboxylase component that catalyzes the transfer of the carboxyl group from CO 2 - -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 [ 14 C]acetyl CoA and malonyl CoA, ( c ) binds labeled acetyl CoA and malonyl CoA, and ( d ) catalyzes the decarboxylation of CO 2 - -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.

Bibliography

Alberts, A. W., Gordon, S. G., & Vagelos, P. R. (1971). Acetyl CoA Carboxylase: The Purified Transcarboxylase Component. Proceedings of the National Academy of Sciences, 68(6), 1259â1263.

Authors 3

Alfred W. Alberts (first)
Stuart G. Gordon (additional)
P. Roy Vagelos (additional)

References 0 Referenced 28

None

Dates

Type	When
Created	19 years, 3 months ago (May 31, 2006, 2:29 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 10:27 a.m.)
Indexed	1 year, 10 months ago (Oct. 17, 2023, 6:31 p.m.)
Issued	54 years, 3 months ago (June 1, 1971)
Published	54 years, 3 months ago (June 1, 1971)
Published Online	54 years, 3 months ago (June 1, 1971)
Published Print	54 years, 3 months ago (June 1, 1971)

Funders 0

None

BibTeX

@article{Alberts_1971, title={Acetyl CoA Carboxylase: The Purified Transcarboxylase Component}, volume={68}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.68.6.1259}, DOI={10.1073/pnas.68.6.1259}, number={6}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Alberts, Alfred W. and Gordon, Stuart G. and Vagelos, P. Roy}, year={1971}, month=jun, pages={1259–1263} }

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  "abstract": "<jats:p>\n            Acetyl CoA carboxylase of\n            <jats:italic>Escherichia coli</jats:italic>\n            has been resolved into three functionally dissimilar proteins: (\n            <jats:italic>1</jats:italic>\n            ) biotin-carboxyl carrier protein (BCCP); (\n            <jats:italic>2</jats:italic>\n            ) a biotin carboxylase component that catalyzes the Mn-ATP-dependent carboxylation of BCCP to form CO\n            <jats:sub>2</jats:sub>\n            <jats:sup>-</jats:sup>\n            -BCCP; and (\n            <jats:italic>3</jats:italic>\n            ) a transcarboxylase component that catalyzes the transfer of the carboxyl group from CO\n            <jats:sub>2</jats:sub>\n            <jats:sup>-</jats:sup>\n            -BCCP to acetyl CoA to form malonyl CoA.\n          </jats:p>\n          <jats:p>\n            The transcarboxylase has been purified 1700-fold. Evidence that this protein catalyzes the transcarboxylase step includes the demonstration that it (\n            <jats:italic>a</jats:italic>\n            ) catalyzes the carboxylation of BCCP, (\n            <jats:italic>b</jats:italic>\n            ) catalyzes the BCCP-dependent exchange between [\n            <jats:sup>14</jats:sup>\n            C]acetyl CoA and malonyl CoA, (\n            <jats:italic>c</jats:italic>\n            ) binds labeled acetyl CoA and malonyl CoA, and (\n            <jats:italic>d</jats:italic>\n            ) catalyzes the decarboxylation of CO\n            <jats:sub>2</jats:sub>\n            <jats:sup>-</jats:sup>\n            -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.\n          </jats:p>",
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