Purification and properties of a carbonyl reductase useful for production of ethyl (S)-4-chloro-3-hydroxybutanoate from Kluyveromyces lactis.
A novel carbonyl reductase (KLCR1) that reduced ethyl 4-chloroacetoacetate (ECAA) to synthesize ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-ECHB) was purified from Kluyveromyces lactis. KLCR1 catalyzed the NADPH-dependent reduction of ECAA enantioselectively but not the oxidation of (S)-ECHB. From partial amino acid sequences, KLCR1 was suggested to be an alpha subunit of fatty acid synthase (FAS) but did not have FAS activity.
D000090:Acetoacetates / Q000378:metabolism; D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification*; D000449:Aldehyde Reductase; D000074408:Aldo-Keto Reductases; D002087:Butyrates / Q000378:metabolism*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007716:Kluyveromyces / Q000201:enzymology* / Q000378:metabolism; D008968:Molecular Conformation; D008970:Molecular Weight; D011479:Protamines / Q000737:chemistry; D013379:Substrate Specificity; D014462:Ultrafiltration
D000090:Acetoacetates; D002087:Butyrates; D011479:Protamines; C121244:ethyl 4-chloro-3-hydroxybutanoate; D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase