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Article

Three hTIM mutants that provide new insights on why TIM is a dimer.

Journal of molecular biology - 29 Mar 1996

Mainfroid V, Terpstra P, Beauregard M, Frère J M, Mande S C, Hol W G, Martial J A, Goraj K

Abstract excerpt

Human triosephosphate isomerase (hTIM), a dimeric enzyme, was altered by site-directed mutagenesis in order to determine whether it can be dissociated into monomers. Two hTIM mutants were produced, in which a glutamine residue was substituted for either Met14 or Arg98, both of which are interface residuces. These substitutions strongly interfere with TIM subunit association, since these mutant TIMs appear to...

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Topics

Amino Acid Sequence
Humans
Kinetics
Models, Molecular
Molecular Sequence Data
Molecular Weight
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Mutation

Protein Conformation

Protein Denaturation

Thermodynamics

Triose-Phosphate Isomerase

Source

Identifiers

PMID: 8609635
DOI: 10.1006/jmbi.1996.0174

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Three hTIM mutants that provide new insights on why TIM is a dimer.PMID 8609635Read ↗

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