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Article

Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.

Biochemistry - 27 Aug 2013

Zhai Xiang, Amyes Tina L, Wierenga Rik K, Loria J Patrick, Richard John P

Abstract excerpt

Triosephosphate isomerase (TIM) catalyzes the isomerization of dihydroxyacetone phosphate to form d-glyceraldehyde 3-phosphate. The effects of two structural mutations in TIM on the kinetic parameters for catalysis of the reaction of the truncated substrate glycolaldehyde (GA) and the activation of this reaction by phosphite dianion are reported. The P168A mutation results in similar 50- and 80-fold decreases in...

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Identifiers

PMID: 23909928
DOI: 10.1021/bi401019h
PMCID: PMC3787511

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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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