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Article

Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site.

The Journal of biological chemistry - 30 Sept 2005

Fujiwara Kazuko, Toma Sachiko, Okamura-Ikeda Kazuko, Motokawa Yutaro, Nakagawa Atsushi, Taniguchi Hisaaki

Abstract excerpt

Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of alpha-ketoacid dehydrogenase complexes and on H-protein of the glycine cleavage system. The lypoyllysine arm plays a pivotal role in the complexes by shuttling the reaction intermediate and reducing equivalents between the...

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Identifiers

PMID: 16043486
DOI: 10.1074/jbc.M505010200

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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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Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site.PMID 16043486Read ↗

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