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Article

Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase.

The Journal of biological chemistry - 4 Apr 2008

McAndrew Ryan P, Wang Yudong, Mohsen Al-Walid, He Miao, Vockley Jerry, Kim Jung-Ja P

Abstract excerpt

Very-long-chain acyl-CoA dehydrogenase (VLCAD) is a member of the family of acyl-CoA dehydrogenases (ACADs). Unlike the other ACADs, which are soluble homotetramers, VLCAD is a homodimer associated with the mitochondrial membrane. VLCAD also possesses an additional 180 residues in the C terminus that are not present in the other ACADs. We have determined the crystal structure of VLCAD complexed with...

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Identifiers

PMID: 18227065
DOI: 10.1074/jbc.M709135200
PMCID: PMC2431035

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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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