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Article

Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit.

Journal of molecular biology - 20 Jan 2006

Sims Paul A, Menefee Ann L, Larsen Todd M, Mansoorabadi Steven O, Reed George H

Abstract excerpt

Enolase is a dimeric enzyme that catalyzes the interconversion of 2-phospho-D-glycerate and phosphoenolpyruvate. This reversible dehydration is effected by general acid-base catalysis that involves, principally, Lys345 and Glu211 (numbering system of enolase 1 from yeast). The crystal structure of the inactive E211Q enolase shows that the protein is properly folded. However, K345 variants have, thus far, failed...

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Identifiers

PMID: 16309698
DOI: 10.1016/j.jmb.2005.10.050
PMCID: PMC3130340

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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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