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Article

Structures of a constitutively active mutant of human IDH3 reveal new insights into the mechanisms of allosteric activation and the catalytic reaction.

The Journal of biological chemistry - 1 Dec 2022

Chen Xingchen, Sun Pengkai, Liu Yan, Shen Senlin, Ma Tengfei, Ding Jianping

Abstract excerpt

Human NAD-dependent isocitrate dehydrogenase or IDH3 (HsIDH3) catalyzes the decarboxylation of isocitrate into α-ketoglutarate in the tricarboxylic acid cycle. It consists of three types of subunits (α, β, and γ) and exists and functions as the (αβαγ)2 heterooctamer. HsIDH3 is regulated allosterically and/or competitively by numerous metabolites including CIT, ADP, ATP, and NADH. Our previous studies have...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 36375638
DOI: 10.1016/j.jbc.2022.102695
PMCID: PMC9731866

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