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Article

A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase.

Structure (London, England : 1993) - 1 Feb 2006

Machius Mischa, Wynn R Max, Chuang Jacinta L, Li Jun, Kluger Ronald, Yu Daria, Tomchick Diana R, Brautigam Chad A, Chuang David T

Abstract excerpt

The dehydrogenase/decarboxylase (E1b) component of the 4 MD human branched-chain alpha-ketoacid dehydrogenase complex (BCKDC) is a thiamin diphosphate (ThDP)-dependent enzyme. We have determined the crystal structures of E1b with ThDP bound intermediates after decarboxylation of alpha-ketoacids. We show that a key tyrosine residue in the E1b active site functions as a conformational switch to reduce the...

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Identifiers

PMID: 16472748
DOI: 10.1016/j.str.2005.10.009

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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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