Carbamyl Phosphate: an Allosteric Substrate for Aspartate Transcarbamylase of Escherichia Coli

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1968 Aug 1

PMID 4877273

Citations 26

Authors

M R Bethell

K E Smith

J S White

M E Jones

Affiliations

Soon will be listed here.

Citing Articles

Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase.

Fetler L, Tauc P, Baker D, Macol C, Kantrowitz E, Vachette P Protein Sci. 2002; 11(5):1074-81.

PMID: 11967364 PMC: 2373563. DOI: 10.1110/ps.4500102.

Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase.

HELMSTAEDT K, Krappmann S, Braus G Microbiol Mol Biol Rev. 2001; 65(3):404-21, table of contents.

PMID: 11528003 PMC: 99034. DOI: 10.1128/MMBR.65.3.404-421.2001.

Conversion of the allosteric regulatory patterns of aspartate transcarbamoylase by exchange of a single beta-strand between diverged regulatory chains.

Liu L, Wales M, Wild J Biochemistry. 1997; 36(11):3126-32.

PMID: 9115988 PMC: 3233766. DOI: 10.1021/bi962065d.

Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.

Zhou B, SCHACHMAN H Protein Sci. 1993; 2(1):103-12.

PMID: 8443583 PMC: 2142301. DOI: 10.1002/pro.5560020111.

Molecular dynamics simulations and rigid body (TLS) analysis of aspartate carbamoyltransferase: evidence for an uncoupled R state.

Tanner J, Smith P, Krause K Protein Sci. 1993; 2(6):927-35.

PMID: 8318897 PMC: 2142406. DOI: 10.1002/pro.5560020606.

References

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