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Article

The role of lysine-234 in beta-lactamase catalysis probed by site-directed mutagenesis.

Biochemistry - 19 Jun 1990

Ellerby L M, Escobar W A, Fink A L, Mitchinson C, Wells J A

Abstract excerpt

Lys-234 has been postulated to participate in beta-lactamase catalysis by acting as an electrostatic anchor for the C3 carboxylate of penicillins [Herzberg, O., & Moult, J. (1987) Science 236, 694-701]. To test this hypothesis, site-directed mutagenesis was used to convert the Lys-234 in Bacillus licheniformis beta-lactamase into Glu-234 or Ala-234. The wild-type, Glu-234, and Ala-234 beta-lactamases have been...

Topics

Alanine
Bacillus
Base Sequence
Catalysis
DNA, Bacterial
Gene Expression
Glutamates
Glutamic Acid
Hydrogen-Ion Concentration
Kinetics
Lysine
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Penicillin V

Substrate Specificity

beta-Lactamases

Source

Identifiers

PMID: 1974463
DOI: 10.1021/bi00476a022

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1974463-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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