The present disclosure relates to the technical field of biotechnology, in particular to carbonyl reductase mutant and its application. Specifically, the present disclosure provides a carbonyl reductase mutant for catalyzing the preparation of (R)-8-chloro-6-hydroxyoctanoic acid ethyl ester from 8-chloro-6-oxooctanoic acid ethyl ester. The mutant protein is a non natural protein and undergoes mutations in three core amino acids related to enzyme catalytic activity in the initial carbonyl reductase. The advantageous effect of the present disclosure is that the carbonyl reductase mutant provided by the present disclosure has the characteristic of efficiently catalyzing the preparation of the precursor substance (R)-8-chloro-6-hydroxyoctanoic acid from 8-chloro-6-oxooctanoic acid ethyl ester, and can efficiently catalyze the oxidation-reduction reaction of 8-chloro-6-oxooctanoic acid, with a product space-time yield of 99.9 g.Math.L1.Math.h1 or more.

The present disclosure relates to the technical field of biotechnology, in particular to carbonyl reductase mutant and its application. Specifically, the present disclosure provides a carbonyl reductase mutant for catalyzing the preparation of (R)-8-chloro-6-hydroxyoctanoic acid ethyl ester from 8-chloro-6-oxooctanoic acid ethyl ester. The mutant protein is a non natural protein and undergoes mutations in three core amino acids related to enzyme catalytic activity in the initial carbonyl reductase. The advantageous effect of the present disclosure is that the carbonyl reductase mutant provided by the present disclosure has the characteristic of efficiently catalyzing the preparation of the precursor substance (R)-8-chloro-6-hydroxyoctanoic acid from 8-chloro-6-oxooctanoic acid ethyl ester, and can efficiently catalyze the oxidation-reduction reaction of 8-chloro-6-oxooctanoic acid, with a product space-time yield of 99.9 g.Math.L1.Math.h1 or more.

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 chiral compounds.

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 provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme including the capability of reducing 5-((4S)-2-oxo-4-phenyl (1,3-oxazolidin-3-yl))-1-(4-fluorophenyl) pentane-1,5-dione to (4S)-3-[(5S)-5-(4-fluorophenyl)-5-hydroxypentanoyl]-4-phenyl-1,3-oxazolidin-2-one. 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 the intermediate (4S)-3-[(5S)-5-(4-fluorophenyl)-5-hydroxypentanoyl]-4-phenyl-1,3-oxazolidin-2-one in a process for making Ezetimibe.

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

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.