Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant.

doi:10.1002/pro.5560010111

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Article

Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant.

Protein science : a publication of the Protein Society - 1 Jan 1992

Toney M D, Kirsch J F

Abstract excerpt

Primary amines functionally replace lysine 258 by catalyzing both the 1,3-prototropic shift and external aldimine hydrolysis reactions with the inactive aspartate aminotransferase mutant K258A. This finding allows classical Brønsted analyses of proton transfer reactions to be applied to enzyme-catalyzed reactions. An earlier study of the reaction of K258A with cysteine sulfinate (Toney, M.D. & Kirsch, J.F., 1989,...

Topics

Acetates
Amines
Amino Acids
Aspartate Aminotransferases
Aspartic Acid
Catalysis
Cysteine
Formates
Hydrolysis
Lysine
Models, Chemical
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Neurotransmitter Agents

Oxaloacetates

Protons

Recombinant Proteins

Schiff Bases

Substrate Specificity

Source

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Identifiers

PMID: 1339023
DOI: 10.1002/pro.5560010111
PMCID: PMC2142083

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1339023-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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