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

The disclosure provides genetically engineered microorganisms and methods for improved biological production of ethylene glycol and precursors of ethylene glycol. The microorganism of the disclosure produces ethylene glycol or a precursor of ethylene glycol through one or more of 5,10-methylenetetrahydrofolate, oxaloacetate, citrate, malate, and glycine. The disclosure further provides compositions comprising ethylene glycol or polymers of ethylene glycol such as polyethylene terephthalate.

Described herein are an immobilized enzyme, and a preparation method therefor and a use thereof. The immobilized enzyme includes activated PEI and an enzyme covalently bonded to the activated PEI, where the enzyme is selected from any one of a transaminase, a ketoreductase, a monooxygenase, an ammonia lyase, an ene-reductase, an imine reductase, an amino acid dehydrogenase and a nitrilase.

Use of a stereoselective transaminase in the asymmetric synthesis of a chiral amine. In particular, provided is use of a polypeptide in the production of a chiral amine or a downstream product using a chiral amine as a precursor. Further provided is a method for producing a chiral amine, comprising culturing a strain expressing the polypeptide so as to obtain a chiral amine. Further provided are novel prochiral compounds, a chiral amine production strain and a method for constructing the chiral amine production strain. The stereoselective transaminase has a broad substrate spectrum and thus has a broad application potential in the preparation of a chiral amine.

Disclosed are transaminase (TA) enzymes and nucleic acids encoding them. In some cases, the transaminase enzymes are non-natural, engineered transaminases. Also disclosed are biosynthetic methods and engineered microorganisms that enhance or improve the biosynthesis of 6-aminocaproate, hexamethylenediamine, caproic acid, caprolactone, or caprolactam. The engineered microorganisms include exogenous TA and in some cases engineered TA.

A novel process is provided for the efficient preparation of an asymmetric compound of structural formula I: ##STR00001##
employing dynamic kinetic resolution (DKR). The DKR process involves an enzymatic enantioselective amination reaction catalyzed by transaminases. The process can be used to manufacture key intermediates in the preparation of poly (ADP-ribose) polymerase (PARP) inhibitors which may be useful for the treatment of cancer.

This document describes biochemical pathways for producing adipyl-[acp] and either hexanoic acid or acetic acid from a long chain acyl-[acp] such as dodecanoyl-[acp] or octanoyl-[acp] using a polypeptide having pimeloyl-[acp] synthase activity and biochemical pathways for converting adipyl-[acp] and/or hexanoic acid to one of more of adipic acid, 6-aminohexanoic acid, 6-hydroxyhexanoic acid, hexamethylenediamine, caprolactam, and 1,6-hexanediol.

Recombinant microorganisms comprising at least one exogenous nucleic acid sequence and capable of producing adipate semialdehyde are provided. Adipate semialdehyde may be produced in a synthesis pathway utilizing a single thiolase reaction. Adipate semialdehyde may also be produced from intermediates consisting of alpha, omega difunctional aliphatic organic molecules. Methods of using recombinant microorganisms to produce 6-aminocaproic acid, adipic acid, hexamethylenediamine and 1.6-hexanediol are also provided.

Disclosed are biosynthetic methods and engineered microorganism that enhance or improve the biosynthesis of hexamethylenediamine, caproic acid or caprolactam. The engineered microorganisms include selected aldehyde dehydrogenase activity.

This disclosure relates to strategies for in vivo production of certain carbon-based products, for example, aminated aliphatic compounds having a carbon chain length of C5-C19.