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Article

Function of the conserved triad residues in the class C beta-lactamase from Citrobacter freundii GN346.

FEBS letters - 1 Oct 1990

Tsukamoto K, Nishida N, Tsuruoka M, Sawai T

Abstract excerpt

The conserved KTG triad in the class C beta-lactamase from Citrobacter freundii GN346 was examined as to its function by means of site-directed mutagenesis. The following conversions were performed; Lys-315 to arginine, alanine or glutamic acid, Thr-316 to valine, and Gly-317 to alanine, proline or isoleucine. The resultant mutant enzymes revealed that a basic amino acid at position 315 and a small uncharged...

Topics

Amino Acids
Binding Sites
Cephalosporins
Citrobacter
Escherichia coli
Hydrogen-Ion Concentration
Kinetics
Mutation
Penicillins
beta-Lactamases

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Identifiers

PMID: 2226810
DOI: 10.1016/0014-5793(90)80416-g

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2226810-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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