Codexis, Inc.

Sandoz Gmbh

Catalytica, Inc.

Catalytica Pharmaceuticals, Inc.

Pfizer Corporation

John M Gruber

Gjalt W Huisman

Emily Mundorff

Charlene Ching

Jack S Liang

Stephane J Jenne

Anke Krebber

Steven James Collier

Christopher K Savile

Lisa Marie Newman

Roger Arthur Sheldon

S Christopher Davis

James Joseph LaLonde

John H Grate

John D Munger, Jr

David R Gray

Steven K Ma

Li A Wang

Jian Ding

Xiyun Zhang

Benjamin Mijts

Michael D Clay

Jagadeesh Mavinahalli

Robert L Carney

Sheela Muley

Jeffrey Colbeck

Alfred S Lui

Jun Zhu

Robert Seemayer

Fred Kuhnen

James LaLonde

A Ray Bulls

Gjalt W Hiusman

Steven J Collier

Emily Mundorrf

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.

Ketoreductase polypeptides for the reduction of acetophenones

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.

Engineered ketoreductase polypeptides

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)&#x2014;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. 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.

Polynucleotides encoding ketoreductase polypeptides for reduction of acetophenones

Methods of using ketoreductase polypeptides for reduction of acetophenones

Polynucleotides encoding engineered ketoreductase polypeptides

Ketoreductases and uses thereof

Growing community of inventors

El Dorado Hills, CA, United States of America

John M Gruber