Journal of Organic Chemistry p. 1526 - 1532 (1992)
Update date:2022-08-05
Topics:
Bradshaw, Curt W.
Fu, Hong
Shen, Gwo-Jenn
Wong, Chi-Huey
A new alcohol dehydrogenase from Pseudomonas sp. strian PED has been isolated and characterized.The enzyme exhibits a broad substrate specificity, accepting aromatic, cyclic, and aliphatic compounds as substrates.The Km values were determined as 525 μM for NAD and 75 μM for 2-propanol with a specific activity of 36 U/mg.The kinetic mechanism is ordered bi-bi with the cofactor binding first and releasing last.The enzyme transfers the pro-R hydride of NADH to the si face of carbonyl compounds to yield (R) alcohols.Synthetic-scale reductions of a number of representative compounds were carried out in high enentiomeric excess with in situ regeneration of NADH using 2-propanol as the hydride source and the same enzyme as catalyst.
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