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Article

Identification of a long-range protein network that modulates active site dynamics in extremophilic alcohol dehydrogenases.

The Journal of biological chemistry - 17 May 2013

Nagel Zachary D, Cun Shujian, Klinman Judith P

Abstract excerpt

A tetrameric thermophilic alcohol dehydrogenase from Bacillus stearothermophilus (ht-ADH) has been mutated at an aromatic side chain in the active site (Trp-87). The ht-W87A mutation results in a loss of the Arrhenius break seen at 30 °C for the wild-type enzyme and an increase in cold lability that is attributed to destabilization of the active tetrameric form. Kinetic isotope effects (KIEs) are nearly...

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Identifiers

PMID: 23525111
DOI: 10.1074/jbc.M113.453951
PMCID: PMC3656266

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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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