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Article

An acidic residue buried in the dimer interface of isocitrate dehydrogenase 1 (IDH1) helps regulate catalysis and pH sensitivity.

The Biochemical journal - 28 Aug 2020

Luna Lucas A, Lesecq Zachary, White Katharine A, Hoang An, Scott David A, Zagnitko Olga, Bobkov Andrey A, Barber Diane L, Schiffer Jamie M, Isom Daniel G, Sohl Christal D

Abstract excerpt

Isocitrate dehydrogenase 1 (IDH1) catalyzes the reversible NADP+-dependent conversion of isocitrate to α-ketoglutarate (αKG) to provide critical cytosolic substrates and drive NADPH-dependent reactions like lipid biosynthesis and glutathione regeneration. In biochemical studies, the forward reaction is studied at neutral pH, while the reverse reaction is typically characterized in more acidic buffers. This led us...

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Identifiers

PMID: 32729927
DOI: 10.1042/BCJ20200311
PMCID: PMC7996970

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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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