4E12

Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductase

Summary for 4E12

• Entry DOI: 10.2210/pdb4e12/pdb
• Related: 4DYD 4E13
• Descriptor: Diketoreductase, GLYCEROL, PENTAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: oxidoreductase, nadh
• Biological source: Acinetobacter baylyi
• Total number of polymer chains: 1
• Total formula weight: 31253.18

Authors

Lu, M.,White, M.A.,Huang, Y.,Wu, X.,Liu, N.,Cheng, X.,Chen, Y. (deposition date: 2012-03-05, release date: 2012-11-14, Last modification date: 2023-11-08)

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

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

Experimental method

X-RAY DIFFRACTION (1.93 Å)