Abstract:
Provided herein are novel, synthetic polypeptides having, for example, acyl-acyl carrier protein (ACP) thioesterase (TE) activity, including polypeptides that convert pimeloyl-ACP to pimelic acid. In some aspects, the synthetic polypeptides have advantageous enzymatic activity and/or improved substrate specificity relative to a wild type acyl-ACP TE.
Abstract:
Disclosed are materials and methods for managing aerobic biosynthesis. The materials include a fermenter system comprising a fermenter, a microorganism provided to the fermenter, and at least two control loops. The methods are directed to measuring and controlling different oxygen concentrations within the fermenter.
Abstract:
This document describes biochemical pathways for producing pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine or 1,7-heptanediol by forming one or two terminal functional groups, each comprised of carboxyl, amine or hydroxyl group, in a C7 aliphatic backbone substrate. These pathways, metabolic engineering and cultivation strategies described herein rely on the C1 elongation enzymes or homolog associated with coenzyme B biosynthesis.
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 the carbon chain elongation enzymes or homologs thereof associated with the cyclohexane carboxylate biosynthesis from Syntrophus aciditrophicus or 2-aminoadipate lysine biosynthesis.
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.