Novel methods for the in vivo production of phenol from renewable substrates using a recombinant microorganism (FIG. 1). Additionally, methods for the in vivo production of catechol and cis,cis-muconic acid from renewable substrates using a recombinant microorganism are disclosed. A host cell expresses at least one gene encoding a polypeptide that possesses isochorismate synthase activity, at least one gene encoding a polypeptide that possesses isochorismate pyruvate lyase activity, and at least one gene encoding a polypeptide that possesses salicylic acid decarboxylase activity. In the case of catechol, the host cell must additionally express at least one gene encoding a polypeptide that possesses phenol 2-monooxygenase activity. In the case of cis,cis-muconic acid, the host cell must additionally express at least one gene encoding a polypeptide that possesses phenol 2-monooxygenase activity and at least one gene encoding a polypeptide that possesses catechol-1,2-dioxygenase activity.

A process of forming a side-chain-functionalized polyhydroxyalkanoate (PHA) material is disclosed. The process includes forming a PHA material having a vinyl-terminated side-chain from a vinyl-terminated fatty acid via a bacterial fermentation process. The process also includes forming a PHA material having a hydroxyl-terminated side-chain from the PHA material having the vinyl-terminated side-chain. The process further includes chemically reacting the PHA material having the hydroxyl-terminated side-chain with 1,4-phenylenedimethanethiol or a chlorocoumarin or 2-furoyl chloride to form a side-chain-functionalized PHA material having a side-chain with a terminal cross-linkable group (e.g., thiol, coumarin, or furoyl group).

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. 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. 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 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. 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. 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 chiral compounds.