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Article

Differential active site loop conformations mediate promiscuous activities in the lactonase SsoPox.

PloS one - 1 Jan 2013

Hiblot Julien, Gotthard Guillaume, Elias Mikael, Chabriere Eric

Abstract excerpt

Enzymes are proficient catalysts that enable fast rates of Michaelis-complex formation, the chemical step and products release. These different steps may require different conformational states of the active site that have distinct binding properties. Moreover, the conformational flexibility of the active site mediates alternative, promiscuous functions. Here we focused on the lactonase SsoPox from Sulfolobus...

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Identifiers

PMID: 24086491
DOI: 10.1371/journal.pone.0075272
PMCID: PMC3781021

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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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