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Article

Substrate-induced conformational change and isomerase activity of dienelactone hydrolase and its site-specific mutants.

Chembiochem : a European journal of chemical biology - 23 Jul 2012

Walker Ian, Hennessy James E, Ollis David L, Easton Christopher J

Abstract excerpt

Studies of the interactions of dienelactone hydrolase (DLH) and its mutants with both E and Z dienelactone substrates show that the enzyme exhibits two different conformational responses specific for hydrolysis of each of its substrate isomers. DLH facilitates hydrolysis of the Z dienelactone through an unusual charge-relay system that is initiated by interaction between the substrate carboxylate and an enzyme...

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Source

Identifiers

PMID: 22761053
DOI: 10.1002/cbic.201200232

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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