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Article

Modelling allosteric processes in E coli aspartate transcarbamylase.

Biochimie - 1 Aug 1990

Cherfils J, Vachette P, Janin J

Abstract excerpt

The allosteric properties of aspartate transcarbamylase from E coli have been investigated by a combination of genetic, biochemical and structural studies. Based on the X-ray structures of the enzyme in T and R state established by Lipscomb et al, we have analyzed the interactions between the 12 polypeptide chains and have identified subunit interfaces that play a major part in the allosteric mechanism: the c1c4...

Topics

Allosteric Regulation
Aspartate Carbamoyltransferase
Escherichia coli
Models, Molecular
Mutation
Protein Conformation
Substrate Specificity
X-Ray Diffraction

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 2126466
DOI: 10.1016/0300-9084(90)90125-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2126466-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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