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Article

Thermodynamic profiles of penicillin G hydrolysis catalyzed by wild-type and Met----Ala168 mutant penicillin acylases from Kluyvera citrophila.

Biochimica et biophysica acta - 9 Feb 1990

Martín J, Prieto I, Barbero J L, Pérez-Gil J, Mancheño J M, Arche R

Abstract excerpt

The Met-168 residue in penicillin acylase from Kluyvera citrophila was changed to Ala by oligonucleotide site-directed mutagenesis. The Ala-168 mutant exhibited different substrate specificity than wild-type and enhanced thermal stability. The thermodynamic profiles for penicillin G hydrolysis ca...

Topics

Alanine
Amidohydrolases
Binding Sites
Enterobacteriaceae
Hydrogen-Ion Concentration
Hydrolysis
Kinetics
Methionine
Mutation
Penicillin Amidase
Penicillin G
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Engineering

Substrate Specificity

Thermodynamics

Source

Identifiers

PMID: 2306469
DOI: 10.1016/0167-4838(90)90158-c

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2306469-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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