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Article

Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I.

Journal of molecular biology - 8 Jun 2007

Yun Mi-Kyung, Nourse Amanda, White Stephen W, Rock Charles O, Heath Richard J

Abstract excerpt

AnsA is the cytoplasmic asparaginase from Escherichia coli involved in intracellular asparagine utilization. Analytical ultracentifugation and X-ray crystallography reveal that AnsA forms a tetrameric structure as a dimer of two intimate dimers. Kinetic analysis of the enzyme reveals that AnsA is positively cooperative, displaying a sigmoidal substrate dependence curve with an [S](0.5) of 1 mM L-asparagine and a...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17451745
DOI: 10.1016/j.jmb.2007.03.061
PMCID: PMC1991333

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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