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Article

Detection of an enzyme bound gamma-glutamyl acyl ester of carbamyl phosphate synthetase of Escherichia coli.

FEBS letters - 14 Dec 1992

Lusty C J

Abstract excerpt

E. coli carbamyl phosphate synthetase binds 0.2-0.4 mol equivalents of glutamine in an acid resistant form. The bound material is quantitatively released as glutamate by weak base hydrolysis and as a mixture of 12% glutamate, 10% gamma-glutamylhydroxamate, and 70% pyrrollidonecarboxylic acid by hydrolysis with hydroxylamine. These results provide direct evidence for a gamma-glutamyl acyl ester on the enzyme. The...

Topics

Acids
Binding Sites
Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)
Cysteine
Escherichia coli
Esters
Glutamates
Glutamine
Hydrolysis
Hydroxamic Acids
Kinetics
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Pyrrolidonecarboxylic Acid

Serine

Source

Identifiers

PMID: 1459243
DOI: 10.1016/0014-5793(92)80959-k

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1459243-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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