4DYD

Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductase

Summary for 4DYD

Entry DOI	10.2210/pdb4dyd/pdb
Descriptor	Diketoreductase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, GLYCEROL, ... (6 entities in total)
Functional Keywords	oxidoreductase, nadh
Biological source	Acinetobacter baylyi
Total number of polymer chains	1
Total formula weight	32136.62
Authors	Lu, M.,White, M.A.,Huang, Y.,Wu, X.,Liu, N.,Cheng, X.,Chen, Y. (deposition date: 2012-02-28, release date: 2012-11-14, Last modification date: 2024-03-20)
Primary citation	Lu, M.,Huang, Y.,White, M.A.,Wu, X.,Liu, N.,Cheng, X.,Chen, Y. Dual catalysis mode for the dicarbonyl reduction catalyzed by diketoreductase Chem.Commun.(Camb.), 48:11352-11354, 2012 Cited by PubMed Abstract: Diketoreductase catalyzes a two-step bioreduction on a dicarbonyl substrate through a novel dual catalysis mode, in which random hydride attack simultaneously forms two mono-carbonyl intermediates, and subsequently distinct catalytic sites are responsible for the reductions of respective carbonyl group of the intermediates to yield the final dihydroxy product. PubMed: 23073461 DOI: 10.1039/c2cc36334h PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation