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Alexander Brett Foster

Bio: Alexander Brett Foster is an academic researcher from Wilmington University. The author has contributed to research in topics: Cupriavidus & Pimelic acid. The author has an hindex of 3, co-authored 13 publications receiving 19 citations.

Papers
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Patent
21 Jul 2017
TL;DR: In this paper, genome-scale attenuation or knockout strategies for directing carbon flux to certain carbon-based building blocks within the 7-aminoheptanoic acid (7-AHA) and 6 -aminohexanoic acids (6- AHA) biosynthesis pathways are discussed.
Abstract: This disclosure relates to genome-scale attenuation or knockout strategies for directing carbon flux to certain carbon based building blocks within the 7-aminoheptanoic acid (7-AHA) and 6-aminohexanoic acid (6-AHA) biosynthesis pathways, for example, to achieve reduced flux to unwanted side products while achieving increased production of desired intermediates and end products. This disclosure also relates to non-naturally occurring mutant bacterial strains comprising one or more gene disruptions in aldehyde reductase and/or aldehyde dehydrogenase genes that are generated to direct carbon flux to certain carbon based building blocks. This disclosure further relates to a method for enhancing production of carbon based building blocks by generating non-naturally occurring mutant bacterial strains, culturing said mutant bacterial strains in the presence of suitable substrates or under desired growth conditions, and substantially purifying the desired end product.

6 citations

Patent
25 Jul 2017
TL;DR: In this article, the authors describe biochemical pathways for producing a difunctional product having an odd number of carbon atoms in vitro or in a recombinant host, or salts or derivatives thereof, by forming two terminal functional groups selected from carboxyl, amine, formyl, and hydroxyl groups in an aliphatic carbon chain backbone.
Abstract: This document describes biochemical pathways for producing a difunctional product having an odd number of carbon atoms in vitro or in a recombinant host, or salts or derivatives thereof, by forming two terminal functional groups selected from carboxyl, amine, formyl, and hydroxyl groups in an aliphatic carbon chain backbone having an odd number of carbon atoms synthesized from (i) acetyl-CoA and propanedioyl-CoA via one or more cycles of methyl ester shielded carbon chain elongation or (ii) propanedioyl-[acp] via one or more cycles of methyl ester shielded carbon chain elongation. The biochemical pathways and metabolic engineering and cultivation strategies described herein rely on enzymes or homologs accepting methyl ester shielded aliphatic carbon chain backbones and maintaining the methyl ester shield for at least one further enzymatic step following one or more cycles of methyl ester shielded carbon chain elongation.

5 citations

Patent
25 Jul 2017
TL;DR: In this article, the authors proposed methods for regulating biosynthesis of at least one of the following C7 building blocks using a pathway having a pimeloyl-ACP intermediate, the method including the step of downregulating the activity of BioF.
Abstract: Disclosed are methods for regulating biosynthesis of at least one of pimelic acid, 7-aminoheptanoic acid, 7-hydroxyheptanoic acid, heptamethylenediamine, 7-arninoheiptanol and 1,7-heptanediol (C7 building blocks) using a pathway having a pimeloyl-ACP intermediate, the method including the step of downregulating the activity of BioF Also disclosed are recombinant hosts by fermentation in which the above methods are performed Further disclosed are recombinant hosts for producing pimeloyl-ACP, the recombinant host including a deletion of a bioF gene

3 citations

Patent
16 Jun 2015
TL;DR: In this article, biochemical pathways for producing 2,4-pentadienoyl-CoA by forming one or two terminal functional groups, comprised of carboxyl or hydroxyl group, in a C5 backbone substrate such as glutaryl-coA, glutaryl-[acp] or glutarate methyl ester.
Abstract: This document describes biochemical pathways for producing 2,4-pentadienoyl-CoA by forming one or two terminal functional groups, comprised of carboxyl or hydroxyl group, in a C5 backbone substrate such as glutaryl-CoA, glutaryl-[acp] or glutarate methyl ester. 2,4-pentadienoyl-CoA can be enzymatically converted to 1,3-butadiene.

2 citations

Patent
03 Oct 2019
TL;DR: In this paper, synthetic polypeptides having acyl-acyl carrier protein (ACP) thioesterase (TE) activity were presented, which converted pimeloyl-ACP to pimelic acid.
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.

1 citations


Cited by
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Patent
16 Jun 2015
TL;DR: In this article, the authors describe biochemical pathways for producing 2,3-dehydroadipyl-CoA methyl ester from precursors such as 2-oxoglutarate using one or more of a fatty acid O-methyltransferase, a thioester enzyme, a CoA-transferase and a coA ligase.
Abstract: This document describes biochemical pathways for producing 2,3-dehydroadipyl-CoA methyl ester from precursors such as 2-oxoglutarate using one or more of a fatty acid O-methyltransferase, a thioesterase, a CoA-transferase and a CoA ligase, as well as recombinant hosts expressing one or more of such enzymes. 2,3-dehydroadipyl-CoA methyl ester can be enzymatically converted to adipyl-CoA using a trans-2-enoyl-CoA reductase, and a methylesterase, which in turn can be enzymatically converted to adipic acid, 6-aminohexanoate, 6-hydroxyhexanoate, caprolactam, hexamethylenediamine, or 1,6-hexanediol.

15 citations

Patent
21 Jul 2017
TL;DR: In this paper, genome-scale attenuation or knockout strategies for directing carbon flux to certain carbon-based building blocks within the 7-aminoheptanoic acid (7-AHA) and 6 -aminohexanoic acids (6- AHA) biosynthesis pathways are discussed.
Abstract: This disclosure relates to genome-scale attenuation or knockout strategies for directing carbon flux to certain carbon based building blocks within the 7-aminoheptanoic acid (7-AHA) and 6-aminohexanoic acid (6-AHA) biosynthesis pathways, for example, to achieve reduced flux to unwanted side products while achieving increased production of desired intermediates and end products. This disclosure also relates to non-naturally occurring mutant bacterial strains comprising one or more gene disruptions in aldehyde reductase and/or aldehyde dehydrogenase genes that are generated to direct carbon flux to certain carbon based building blocks. This disclosure further relates to a method for enhancing production of carbon based building blocks by generating non-naturally occurring mutant bacterial strains, culturing said mutant bacterial strains in the presence of suitable substrates or under desired growth conditions, and substantially purifying the desired end product.

6 citations

Patent
16 Jun 2015
TL;DR: In this paper, biochemical pathways for producing 2,4-pentadienoyl-CoA by forming one or two terminal functional groups, comprised of carboxyl or hydroxyl group, in a C5 backbone substrate such as glutaryl-coA, glutaryl-[acp] or glutarate methyl ester.
Abstract: This document describes biochemical pathways for producing 2,4-pentadienoyl-CoA by forming one or two terminal functional groups, comprised of carboxyl or hydroxyl group, in a C5 backbone substrate such as glutaryl-CoA, glutaryl-[acp] or glutarate methyl ester. 2,4-pentadienoyl-CoA can be enzymatically converted to 1,3-butadiene.

2 citations

Patent
03 Oct 2019
TL;DR: In this paper, synthetic polypeptides having acyl-acyl carrier protein (ACP) thioesterase (TE) activity were presented, which converted pimeloyl-ACP to pimelic acid.
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.

1 citations

Patent
03 Oct 2019
TL;DR: In this paper, a transaminase from Chromobacterium violaceum from pimelate semialdehyde using alanine, GABA (gamma aminobutyric acid) or 6-ACA as amino donors was used.
Abstract: 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. Specifically, 7-aminoheptanoic acid is produced using a transaminase from Chromobacterium violaceum from pimelate semialdehyde using alanine, GABA (gamma aminobutyric acid) or 6-ACA as amino donors.

1 citations