Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 60 ·No. 4 ·1968-08-00 ·Pages 1442-9

Bethell MR, Smith KE, White JS, Jones ME

Abstract

暂无摘要

MeSH Terms

Aspartic Acid Binding Sites Carbamates Escherichia coli/enzymology Nucleotides Phosphates Transferases

Chemicals

Carbamates Nucleotides Phosphates Aspartic Acid Transferases

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Bethell M R

Smith K E

White J S

Jones M E

References (16)

16 references, click to expand

Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase.
Biochemistry. 1965 Jun;4(6):1054-62 PMID: 5320387
Comparison of experimental binding data and theoretical models in proteins containing subunits.
Biochemistry. 1966 Jan;5(1):365-85 PMID: 5938952
The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits.
J Biol Chem. 1967 Jun 25;242(12):2886-92 PMID: 5338508
Substrate- and inhibitor-induced changes in the optical rotatory dispersion of aspartate transcarbamylase.
Nature. 1966 Jul 30;211(5048):497-501 PMID: 5967490
Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits.
Biochemistry. 1968 Feb;7(2):531-8 PMID: 4868539
Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands.
Biochemistry. 1968 Feb;7(2):538-52 PMID: 4868540
Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of experimental data in terms of the model of Monod, Wyman, and Changeux.
Biochemistry. 1968 Feb;7(2):553-61 PMID: 4868541
Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism.
J Biol Chem. 1956 Aug;221(2):757-70 PMID: 13357469
The enzymology of control by feedback inhibition.
J Biol Chem. 1962 Mar;237:891-6 PMID: 13897943
END-PRODUCT INHIBITION OF ASPARTATE TRANSCARBAMYLASE IN VARIOUS SPECIES.
Arch Biochem Biophys. 1964 Mar;104:438-47 PMID: 14161013
ASPARTATE TRANSCARBAMYLASE, AN ENZYME DESIGNED FOR FEEDBACK INHIBITION.
Fed Proc. 1964 May-Jun;23:727-35 PMID: 14191980
DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.
Ann N Y Acad Sci. 1964 Dec 28;121:404-27 PMID: 14240539
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.
J Mol Biol. 1965 May;12:88-118 PMID: 14343300
Measurement of cell growth in tissue culture with a phenol reagent (folin-ciocalteau).
Proc Soc Exp Biol Med. 1956 Feb;91(2):305-7 PMID: 13297784
Studies on the biosynthesis of carbamylaspartic acid.
J Biol Chem. 1956 May;220(1):57-70 PMID: 13319326
KINETICS OF REGULATORY ENZYMES. KINETIC ORDER OF THE YEAST DIPHOSPHOPYRIDINE NUCLEOTIDE ISOCITRATE DEHYDROGENASE REACTION AND A MODEL FOR THE REACTION.
J Biol Chem. 1965 Jun;240:2682-90 PMID: 14304886

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

DOI

10.1073/pnas.60.4.1442

Published

1968-08-00

Pages

1442-9

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC224939

Subset

External Links

PubMed source DOI: 10.1073/pnas.60.4.1442 PMC Full Text View journal details

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Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli.

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