The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize a variety of chiral compounds.

The present disclosure relates to engineered ketoreductase polypeptides for the preparation of hydroxyl substituted carbamate compounds, and polynucleotides, vectors, host cells, and methods of making and using the ketoreductase polypeptides.

The invention relates to ketoreductases and the use thereof. The ketoreductases of the invention are particularly useful for enzymatically catalyzing the reduction of ketones to chiral secondary alcohols.

An object of the present invention is to provide a novel method capable of producing rosuvastatin calcium and intermediates therefor efficiently, inexpensively and with high purity. The present invention provides a method of efficiently producing rosuvastatin calcium and intermediates therefor having a high purity at an industrial scale, without using an extremely low temperature reaction or a special asymmetric catalyst.

The disclosure relates to engineered ketoreductase polypeptides and processes of using the polypeptides for production of phenylephrine.

The present disclosure relates to non-naturally occurring polypeptides useful for preparing Ezetimibe, polynucleotides encoding the polypeptides, and methods of using the polypeptides.

A carbonyl reductase mutant and application thereof are provided. Mutation sites of the carbonyl reductase mutant include the 88th, 142nd, 190th, and 193rd positions of the amino acid sequence shown in SEQ ID NO:1. The carbonyl reductase mutant has higher enzymatic activity than wild-type carbonyl reductases. The enzymatic activity of some carbonyl reductase mutants is 50 times that of the wild-type carbonyl reductases. The carbonyl reductase mutant can cause a compound shown in formula I to carry out a reduction reaction shown in the following formula in a liquid reaction system in the presence of coenzymes, can prepare a compound represented by formula II with a conversion rate greater than 99%, a chiral ee value greater than 99%, and a chiral de value greater than 99%.

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Disclosed herein is Candida parapsilosis CGMCC 9630, the carbonyl reductase expressed by said strain and the encoding gene and amino acid sequence thereof, the recombinant expression vector and recombinant expression transformant containing said gene sequence, and use of whole cells of Candida parapsilosis, carbonyl reductase or corresponding recombinant transformant thereof as catalyst in catalyzing asymmetric reduction of prochiral carbonyl compounds, particularly reduction of 6-carbonyl-8-halogenocaprylate to prepare the synthetic precursor of (R)--lipoic acid, (R)-6-hydroxy-8-halogenocaprylate. In comparison to other methods of asymmetric reduction for preparing (R)-6-hydroxy-8-halogenocaprylate, the disclosure has advantages of high substrate concentration, mild reaction conditions, environmental friendship, high yield, and high optical purity of the product, and thus has good prospect in industrial production of (R)---lipoic acid.

The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize a variety of chiral compounds. The engineered ketoreductase polypeptides are optimized for catalyzing the conversion of N-methyl-3-keto-3-(2-thienyl)-1-propanamine to (S)N-methyl-3-hydroxy-3-(2-thienyl)-1-propanamine.

The present disclosure relates to non-naturally occurring polypeptides useful for preparing Ezetimibe, polynucleotides encoding the polypeptides, and methods of using the polypeptides.