1b15
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ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS TERNARY COMPLEX WITH NAD-ACETONE
OverviewOverview
Drosophila alcohol dehydrogenase (DADH) is an NAD+-dependent enzyme that, catalyzes the oxidation of alcohols to aldehydes/ketones. DADH is the, member of the short-chain dehydrogenases/reductases family (SDR) for which, the largest amount of biochemical data has been gathered during the last, three decades. The crystal structures of one binary form (NAD+) and three, ternary complexes with NAD+.acetone, NAD+.3-pentanone and, NAD+.cyclohexanone were solved at 2.4, 2.2, 1. 4 and 1.6 A resolution, respectively. From the molecular interactions observed, the reaction, mechanism could be inferred. The structure of DADH undergoes a, conformational change in order to bind the coenzyme. Furthermore, upon, binding of the ketone, a region that was disordered in the apo form, (186-191) gets ... [(full description)]
About this StructureAbout this Structure
1B15 is a [Single protein] structure of sequence from [Scaptodrosophila lebanonensis] with NAE as [ligand]. Active as [[1]], with EC number [1.1.1.1]. Full crystallographic information is available from [OCA].
ReferenceReference
The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography., Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R, J Mol Biol. 1999 Jun 4;289(2):335-55. PMID:10366509
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