Abstract: This document describes biochemical pathways for producing 7-aminoheptanoic acid using a ?-ketoacyl synthase or a ?-ketothiolase to form an N-acetyl-5-amino-3-oxopentanoyl-CoA intermediate. 7-aminoheptanoic acid can be enzymatically converted to pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol or corresponding salts thereof. This document also describes recombinant microorganisms producing 7-aminoheptanoic acid as well as pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol or corresponding salts thereof.

Abstract: This document describes biochemical pathways for producing 7-aminoheptanoic acid using a ?-ketoacyl synthase or a ?-ketothiolase to form an N-acetyl-5-amino-3-oxopentanoyl-CoA intermediate. 7-aminoheptanoic acid can be enzymatically converted to pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol or corresponding salts thereof. This document also describes recombinant microorganisms producing 7-aminoheptanoic acid as well as pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol or corresponding salts thereof.

Abstract: This document describes biochemical pathways for producing 7-aminoheptanoic acid using a ?-ketoacyl synthase or a ?-ketothiolase to form either a 5-amino-3-oxopentanoyl-[ACP] or 5-amino-3-oxopentanoyl-CoA intermediate. 7-aminoheptanoic acid can be enzymatically converted to pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol or the corresponding salts thereof. This document also describes recombinant microorganisms producing 7-aminoheptanoic acid as well as pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol or the corresponding salts thereof.

Abstract: This document describes biochemical pathways for biosynthesizing a 3-oxo-7-hydroxyheptanoyl-CoA intermediate using a ?-ketothiolase, and enzymatically converting 3-oxo-7-hydroxyheptanoyl-CoA to 7-hydroxyheptanoic acid. —7-hydroxyheptanoic acid can be further enzymatically converted to pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine or 1,7-heptanediol. This document also describes recombinant hosts producing 7-hydroxyheptanoic acid as well as pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine and 1,7-heptanediol.

Abstract: This document describes biochemical pathways for biosynthesizing a 3-oxo-7-hydroxyheptanoyl-CoA intermediate using a ?-ketothiolase, and enzymatically converting 3-oxo-7-hydroxyheptanoyl-CoA to 7-hydroxyheptanoic acid. —7-hydroxyheptanoic acid can be further enzymatically converted to pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine or 1,7-heptanediol. This document also describes recombinant hosts producing 7-hydroxyheptanoic acid as well as pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine and 1,7-heptanediol.

Abstract: This document describes biochemical pathways for producing 7-aminoheptanoic acid using a ?-ketoacyl synthase or a ?-ketothiolase to form either a 5-amino-3-oxopentanoyl-[ACP] or 5-amino-3-oxopentanoyl-CoA intermediate. 7-aminoheptanoic acid can be enzymatically converted to pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol or the corresponding salts thereof. This document also describes recombinant microorganisms producing 7-aminoheptanoic acid as well as pimelic acid, 7-hydroxyheptanoic acid, heptamethylenediamine and 1,7-heptanediol or the corresponding salts thereof.

Abstract: This document describes polypeptides with dual CoA transferase and ?-ketothiolase activities and variants thereof, use of such polypeptides in biosynthetic methods, and non-naturally occurring hosts comprising such polypeptides.

Abstract: The disclosure relates to polypeptides having carboxylic acid reductase (CAR) activity, including enzymes that catalyse the irreversible reduction of carboxylic acids, such as pimelic acid and adipic acid, to their respective semialdehydes. The enzymes have been engineered to have higher activity over a corresponding wild type enzyme. Provided herein are novel polypeptides and uses thereof related to the same.

Abstract: This document describes biochemical pathways for producing isoprene by forming two vinyl groups in a central precursor produced from isobutyryl-CoA, 3-methyl-2-oxopentanoate, or 4-methyl-2-oxopentanoate as well as recombinant hosts for producing isoprene.

Abstract: The document provides methods for biosynthesizing isobutene using one or more isolated enzymes such as one or more of a hydratase such as an enzyme classified under EC 4.2.1.- and a decarboxylating thioesterase, or using recombinant host cells expressing one or more such enzymes.

Abstract: This document describes biochemical pathways for producing adipic acid, caprolactam, 6-aminohexanoic acid, 6-hydroxyhexanoic acid, hexamethylenediamine or 1,6-hexanediol by forming two terminal functional groups, comprised of carboxyl, amine or hydroxyl groups, in a C6 aliphatic backbone substrate. These pathways, metabolic engineering and cultivation strategies described herein rely on CoA-dependent elongation enzymes or analogues enzymes associated with the carbon storage pathways from polyhydroxyalkanoate accumulating bacteria.

Abstract: This document describes biochemical pathways for producing pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol by forming two terminal functional groups, comprised of carboxyl, amine or hydroxyl group, in a C7 aliphatic backbone substrate. These pathways, metabolic engineering and cultivation strategies described herein rely on enzymes or homologs accepting methyl ester shielded dicarboxylic acid substrates.

Abstract: This document describes biochemical pathways for producing butadiene by forming two vinyl groups in a butadiene synthesis substrate. These pathways described herein rely on enzymes such as, inter alia, a decarboxylating thioesterase, cytochrome P450, or dehydratases for the final enzymatic step.

Abstract: This document describes materials and methods for, for example, producing 6-hydroxyhexanoic acid using a ?-ketothiolase or synthase and an alcohol O-acetyltransferase to form a 6-acetyloxy-3-oxohexanoyl-CoA intermediate. This document describes biochemical pathways for producing 6-hydroxyhexanoic acid using a ?-ketothiolase or synthase and an alcohol O-acetyltransferase to form a 6-acetyloxy-3-oxohexanoyl-CoA intermediate. 6-hydroxyhexanoic acid can be enzymatically converted to adipic acid, caprolactam, 6-aminohexanoic acid, hexamethylenediamine or 1,6-hexanediol. This document also describes recombinant hosts producing 6-hydroxyhexanoic acid as well as adipic acid, caprolactam, 6-aminohexanoic acid, hexamethylenediamine and 1,6-hexanediol.

Abstract: This document describes biochemical pathways for producing 4-hydroxybutyrate, 4-aminobutyrate, putrescine or 1,4-butanediol by forming one or two terminal functional groups, comprised of amine or hydroxyl group, in a C5 backbone substrate such as 2-oxoglutarate or L-glutamate.

Abstract: This document describes biochemical pathways that include the production of 3-oxopent-4-enoyl-CoA by condensation of acryloyl-CoA and acetyl-CoA using a ?-ketothiolase with a SER-HIS-HIS catalytic triad. These pathways described herein rely on enzymes such as, inter alia, dehydrogenases, dehydratases and ?-ketothiolases.

Abstract: This document describes biochemical pathways for producing butadiene by forming two vinyl groups in a butadiene synthesis substrate. These pathways described herein rely on enzymes such as, inter alia, a decarboxylating thioesterase, cytochrome P450, or dehydratases for the final enzymatic step.

Abstract: This document describes biochemical pathways that include the production of 3-oxopent-4-enoyl-CoA by condensation of acryloyl-CoA and acetyl-CoA using a ?-ketothiolase with a SER-HIS-HIS catalytic triad. These pathways described herein rely on enzymes such as, inter alia, dehydrogenases, dehydratases and ?-ketothiolases.

Abstract: This document describes materials and methods for, for example, producing 6-hydroxyhexanoic acid using a ?-ketothiolase or synthase and an alcohol O-acetyltransferase to form a 6-acetyloxy-3-oxohexanoyl-CoA intermediate. This document describes biochemical pathways for producing 6-hydroxyhexanoic acid using a ?-ketothiolase or synthase and an alcohol O-acetyltransferase to form a 6-acetyloxy-3-oxohexanoyl-CoA intermediate. 6-hydroxyhexanoic acid can be enzymatically converted to adipic acid, caprolactam, 6-aminohexanoic acid, hexamethylenediamine or 1,6-hexanediol. This document also describes recombinant hosts producing 6-hydroxyhexanoic acid as well as adipic acid, caprolactam, 6-aminohexanoic acid, hexamethylenediamine and 1,6-hexanediol.

Abstract: This document describes biochemical pathways for producing adipic acid, caprolactam, 6-aminohexanoic acid, 6-hydroxyhexanoic acid, hexamethylenediamine or 1,6-hexanediol by forming two terminal functional groups, comprised of carboxyl, amine or hydroxyl groups, in a C6 aliphatic backbone substrate. These pathways, metabolic engineering and cultivation strategies described herein rely on CoA-dependent elongation enzymes or analogues enzymes associated with the carbon storage pathways from polyhydroxyalkanoate accumulating bacteria.