Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 122, Issue -, Pages 44-50Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2015.08.018
Keywords
Aldo-keto reductase; Candida albicans; Asymmetric bioreduction; Chiral alcohol
Funding
- National Basic Research Program of China (973 Program) [2011CB710800]
- Major Program for Key Science and Technology of Zhejiang Province of China [2014C03010]
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An aldo-keto reductase encoding gene caakr was cloned from Candida albicans XP1463 (CCTCC M 2014382), and heterologously expressed in Escherichia coil. The aldo-keto reductase CaAKR is NADH-dependent with a molecular weight of approximately 38.6 kDal including a His(6)-Tag. It is active and stable at 30 degrees C and pH 7.0. The maximal reaction rate (V-max), apparent Michaelis-Menten constant (K-m) and catalytic constant (k(cat)) for t-butyl 6-cyano-(5R)-hydroxy-3-oxohexanoate ((R)-1a) were 11.50 mmol/L min, 1.91 mmol/L and 218.50 min(-1). Besides atorvastatin's chiral synthon t-butyl 6-cyano-(3R,5R)- dihydroxy hexanoate ((R,R)-1b), it can synthesize N,N-2-dimethyl-(3S)-hydroxy-3-(2-thienyl)-1-propanine ((S)9b) and methyl 1-[E]-2-[3-[3-[2-(7-chloro-2-quinoliny) ethenyl] phenyl]-(3S)-hydroxy propy] benzoate ((S)-10b), the chiral intermediates of duloxetine and montelukast, displaying potential applications in pharmaceutical industry. (C) 2015 Elsevier B.V. All rights reserved.
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