A new alcohol dehydrogenase from Pseudomonas sp. strain FED 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 µ for NAD and 75 µ 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 enantiomeric excess with in situ regeneration of NADH using 2-propanol as the hydride source and the same enzyme as catalyst.

No abstract

No abstract

No abstract

No abstract