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Article

Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95.

Biochemistry - 26 Mar 1991

Komives E A, Chang L C, Lolis E, Tilton R F, Petsko G A, Knowles J R

Abstract excerpt

Electrophilic catalysis by histidine-95 in triosephosphate isomerase has been probed by using Fourier transform infrared spectroscopy and X-ray crystallography. The carbonyl stretching frequency of dihydroxyacetone phosphate bound to the wild-type enzyme is known to be 19 cm-1 lower (at 1713 cm-1) than that of dihydroxyacetone phosphate free in solution (at 1732 cm-1), and this decrease in stretching frequency...

Topics

Base Sequence
Binding Sites
Catalysis
Fourier Analysis
Histidine
Kinetics
Models, Molecular
Molecular Sequence Data
Mutation
Spectrophotometry, Infrared
Triose-Phosphate Isomerase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

X-Ray Diffraction

Source

Identifiers

PMID: 2007138
DOI: 10.1021/bi00226a005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2007138-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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