Recombinant microorganisms comprising DNA molecules in a deregulated form which improve the production of cadaverine or N-acetylcadaverine, as well as recombinant DNA molecules and polypeptides used to produce the microorganisms are provided. Said microorganisms comprise an intracellular lysine decarboxylase activity and a deregulated cadaverine export activity, or comprise a decreased cadaverine export activity and an enhanced N-acetylcadaverine forming activity. Processes for the production of cadaverine N-acetylcadaverine using the recombinant microorganisms are also provided.

This document describes biochemical pathways for producing 2-aminopimelate from 2,6-diaminopimelate, and methods for converting 2-aminopimelate to one or more of adipic acid, adipate semialdehyde, caprolactam, 6-aminohexanoic acid, 6-hexanoic acid, hexamethylenediamine, or 1,6-hexanediol by decarboxylating 2-aminopimelate into a six carbon chain aliphatic backbone and enzymatically forming one or two terminal functional groups, comprised of carboxyl, amine or hydroxyl group, in the backbone.

The present disclosure describes biocatalytic processes for producing a product, comprising providing an aqueous stream (AS) comprising at least one fermentable substrate and a gaseous stream (GS) comprising at least one of CO.sub.2/H.sub.2, H.sub.2, methane, and/or CO to a fermentation zone, wherein the GS and AS stream are optionally contacted and/or mixed; the fermentation zone comprising at least one organism capable of metabolizing an AS substrate and a GS substrate, wherein the fermentation operates at conditions to mixotrophically metabolize at least one gaseous substrate in the GS and at least one substrate in the AS, producing the product. The present disclosure also describes compositions comprising an AS, a GS, and an organism, wherein the organism or an equivalent or engineered equivalent thereof is a methanotroph or a hydrogen-metabolizing or CO-metabolizing chemolithotrophic organism, and wherein the organism is capable of mixotrophic metabolism of at least one gaseous substrate in the GS and at least one substrate in the AS. The present disclosure also describes a process wherein said fermentation operates at conditions to mixotrophically metabolize at least H.sub.2 in the gaseous stream and glycerol and lactic acid in the aqueous stream. The present disclosure also describes a system for producing a fermentation or bio-derived product.

This document describes biochemical pathways for producing one or more of pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol by forming one or two terminal functional groups, comprised of carboxyl, amine or hydroxyl groups, in a C7 aliphatic backbone substrate produced from succinate semialdehyde or pyruvate. These pathways, metabolic engineering and cultivation strategies described herein rely on the aldol condensation of succinate semialdehyde and pyruvate.

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 7-hydroxyheptanoate methyl ester and heptanoic acid heptyl ester using one or more of a fatty acid O-methyltransferase, an alcohol O-acetyltransferase, and a monooxygenase, as well as recombinant hosts expressing one or more of such exogenous enzymes. 7-hydroxyheptanoate methyl esters and heptanoic acid heptyl esters can be enzymatically converted to pimelic acid, 7-aminoheptanoate, 7-hydroxyheptanoate, heptamethylenediamine, or 1,7-heptanediol.

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.

The present disclosure describes the engineering of microbial cells for fermentative production of 1,5-diaminopentane and provides novel engineered microbial cells and cultures, as well as related 1,5-diaminopentane production methods.

The present invention discloses an E. coli engineering bacteria producing 1,5-pentanediamine through a whole cell catalysis and its application. The engineering bacteria according to the present invention, is Escherichia coli (E. coli) strain B or its derivative strains with the overexpression of a lysine decarboxylase gene and a proper expression of a lysine-cadaverine antiporter gene cadB. The engineering bacteria according to the present invention is the engineering bacteria producing 1,5-pentanediamine through the whole cell catalysis constructed from Escherichia coli B derivative strains, which has an overexpression of a lysine decarboxylase gene cadA and a proper expression of the lysine-cadaverine antiporter gene cadB. The present invention further discloses a method of producing a 1,5-pentanediamine catalyzed by the engineering bacteria, the yield and production intensity of 1,5-pentanediamine in bio-based production could be significantly improved through the method, hence it could be applied to mass production and convenient for extending applications.

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