Open AccessA novel NADPH‐dependent aldehyde reductase, catalyzing asymmetric reduction of ß‐keto acid esters, from Sporobolomyces salmonicolor : purification and characterization
Author(s) -
Yamada Hideaki,
Shimizu Sakayu,
Kataoka Michihiko,
Sakai Hiromi,
Miyoshi Teruzo
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb03775.x
Subject(s) - aldehyde , chemistry , aldehyde reductase , enzyme , stereospecificity , reductase , ammonium sulfate , yield (engineering) , stereochemistry , biochemistry , catalysis , organic chemistry , materials science , metallurgy
NADPH‐dependent aldehyde reductase (EC 1.1.1.2) was purified 23‐fold with an overall yield of 11% from Sporobolomyces salmonicolor AKU 4429, in 4 steps and, by adding ammonium sulfate, the enzyme was crystallized. The enzyme has a strict requirement for NADPH and irrversibly reduces a number of aldehydes, such as p ‐nitrobenzaldehyde, pyridine‐3‐aldehyde and d ‐glyceraldehyde. Furthermore, it was found that the enzyme catalyses stereospecific reduction of 4‐halo‐3‐oxobutanoate esters to the corresponding ( R )‐4‐halo‐3‐hydroxybutanoate esters, which are promising chiral compounds for the chemical synthesis of l ‐carnitine.