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Article

Substitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity.

European journal of biochemistry - 15 Jan 1995

Vacca R A, Christen P, Malashkevich V N, Jansonius J N, Sandmeier E

Abstract excerpt

In an attempt to change the reaction and substrate specificity of aspartate aminotransferase, several apolar active-site residues were substituted in turn with a histidine residue. Aspartate aminotransferase W140H (of Escherichia coli) racemizes alanine seven times faster (Kcat' = 2.2 x 10(-4) s-1) than the wild-type enzyme, while the aminotransferase activity toward L-alanine was sixfold decreased. X-ray...

Topics

Animals
Aspartate Aminotransferases
Base Sequence
Catalysis
Chickens
Crystallography, X-Ray
Escherichia coli
Histidine
Kinetics
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oligodeoxyribonucleotides

Pyridoxamine

Substrate Specificity

Source

Identifiers

PMID: 7851426
DOI: 10.1111/j.1432-1033.1995.tb20413.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7851426-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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