Title : Molecular docking studies on interaction of diverse retinol structures with human alcohol dehydrogenases predict a broad role in retinoid ligand synthesis.

Pub. Date : 1999 Jul 13

PMID : 10407146






4 Functional Relationships(s)
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Protein Name
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1 The crystal structures of human ADH1B and ADH4 provide the opportunity to examine their active sites for potential binding to many diverse retinol structures using molecular docking algorithms. Vitamin A alcohol dehydrogenase 1B (class I), beta polypeptide Homo sapiens
2 By these criteria, all-trans-retinol, 4-oxo-retinol, and 4-hydroxy-retinol were successfully docked to both ADH1B and ADH4. Vitamin A alcohol dehydrogenase 1B (class I), beta polypeptide Homo sapiens
3 These findings suggest that ADH1B has a limited capacity to metabolize retinols, but that ADH4 is well suited to function in the metabolism of many diverse retinols and is predicted to participate in the synthesis of the active ligands all-trans-retinoic acid, 9-cis-retinoic acid, 3, 4-didehydroretinoic acid, 4-oxo-retinoic acid, and 4-hydroxy-retinoic acid. Vitamin A alcohol dehydrogenase 1B (class I), beta polypeptide Homo sapiens
4 These findings suggest that ADH1B has a limited capacity to metabolize retinols, but that ADH4 is well suited to function in the metabolism of many diverse retinols and is predicted to participate in the synthesis of the active ligands all-trans-retinoic acid, 9-cis-retinoic acid, 3, 4-didehydroretinoic acid, 4-oxo-retinoic acid, and 4-hydroxy-retinoic acid. Vitamin A alcohol dehydrogenase 1B (class I), beta polypeptide Homo sapiens