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Article

Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.

Biochemistry - 31 May 2016

Richard John P, Amyes Tina L, Malabanan M Merced, Zhai Xiang, Kim Kalvin J, Reinhardt Christopher J, Wierenga Rik K, Drake Eric J, Gulick Andrew M

Abstract excerpt

Kinetic parameters are reported for the reactions of whole substrates (kcat/Km, M(-1) s(-1)) (R)-glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP) and for the substrate pieces [(kcat/Km)E·HPi/Kd, M(-2) s(-1)] glycolaldehyde (GA) and phosphite dianion (HPi) catalyzed by the I172A/L232A mutant of triosephosphate isomerase from Trypanosoma brucei brucei (TbbTIM). A comparison with the...

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Identifiers

PMID: 27149328
DOI: 10.1021/acs.biochem.6b00311
PMCID: PMC4934371

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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