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Article

Replacement of active-site lysine-239 of thermostable aspartate aminotransferase by S-(2-aminoethyl)cysteine: properties of the mutant enzyme.

Journal of biochemistry - 1 Jan 1994

Matsushima Y, Kim D W, Yoshimura T, Kuramitsu S, Kagamiyama H, Esaki N, Soda K

Abstract excerpt

The active-site lysine residue of thermostable aspartate aminotransferase, Lys-239, to which the cofactor, pyridoxal 5'-phosphate (PLP), is bound, has been converted to Cys by site-directed mutagenesis. The thiol group of Cys-239 was chemically aminoethylated with ethylenimine. Amino acid analysi...

Topics

Aspartate Aminotransferases
Binding Sites
Cysteine
Enzyme Stability
Escherichia coli
Hydrogen-Ion Concentration
Kinetics
Lysine
Models, Chemical
Mutagenesis, Site-Directed
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Pyridoxal Phosphate

Temperature

Thermodynamics

Source

Identifiers

PMID: 8188615
DOI: 10.1093/oxfordjournals.jbchem.a124283

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8188615-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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