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Article

A proton relay enhances H2O2 sensitivity of GAPDH to facilitate metabolic adaptation.

Nature chemical biology - 1 Feb 2015

Peralta David, Bronowska Agnieszka K, Morgan Bruce, Dóka Éva, Van Laer Koen, Nagy Péter, Gräter Frauke, Dick Tobias P

Abstract excerpt

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is sensitive to reversible oxidative inactivation by hydrogen peroxide (H2O2). Here we show that H2O2 reactivity of the active site thiolate (C152) is catalyzed by a previously unrecognized mechanism based on a dedicated proton relay promoting leaving group departure. Disruption of the peroxidatic reaction mechanism does not affect the glycolytic activity of GAPDH....

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Identifiers

PMID: 25580853
DOI: 10.1038/nchembio.1720

Genes

GAPDH

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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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