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The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule

Autor: C K, Engel, T R, Kiema, J K, Hiltunen, R K, Wierenga

Publikováno v: Journal of molecular biology. 275(5)

The structure of the hexameric rat mitochondrial enoyl-Coenzyme A (CoA) hydratase, co-crystallised with the inhibitor octanoyl-CoA, has been refined at a resolution of 2.4 A. Enoyl-CoA hydratase catalyses the hydration of 2,3-unsaturated enoyl-CoA th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3be1df665075a49ecc6bb7d4ee395c6c
https://pubmed.ncbi.nlm.nih.gov/9480773

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Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket

Autor: C K, Engel, M, Mathieu, J P, Zeelen, J K, Hiltunen, R K, Wierenga

Publikováno v: The EMBO journal. 15(19)

The crystal structure of rat liver mitochondrial enoyl-coenzyme A (CoA) hydratase complexed with the potent inhibitor acetoacetyl-CoA has been refined at 2.5 angstroms resolution. This enzyme catalyses the reversible addition of water to alpha,beta-u

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::405ebbfc07f25c0bae8a18bc5e6f6cf7
https://pubmed.ncbi.nlm.nih.gov/8895557

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