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Methods of producing 6-carbon chemicals using 2,6-diaminopimelate as precursor to 2-aminopimelate

A technology of diaminopimelic acid and aminopimelic acid, applied in biochemical equipment and methods, carbon-nitrogen lyase, carbon-oxygen lyase, etc., can solve the problem of no report

Inactive Publication Date: 2017-04-19
INVISTA TEXTILES (U K) LTD
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

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Problems solved by technology

However, no information was reported using these strategies (Jang et al., Biotechnology & Bioengineering, 2012, 109(10), 2437-2459)

Method used

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  • Methods of producing 6-carbon chemicals using 2,6-diaminopimelate as precursor to 2-aminopimelate
  • Methods of producing 6-carbon chemicals using 2,6-diaminopimelate as precursor to 2-aminopimelate
  • Methods of producing 6-carbon chemicals using 2,6-diaminopimelate as precursor to 2-aminopimelate

Examples

Experimental program
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Effect test

Embodiment 1

[0275] Enzymatic activity of ω-transaminase using adipate semialdehyde as substrate and forming 6-aminocaproic acid

[0276] The nucleotide sequence encoding the His-tag was added to the omega-transaminases from Chromobacterium violaceum, Pseudomonas aeruginosa, Pseudomonas syringae, spheroid Rhodobacter and Vibrio genes (see Figure 20 ), allowing the generation of N-terminally HIS-tagged ω-transaminases. Each of the resulting modified genes was cloned into the pET21a expression vector under the control of the T7 promoter, and each expression vector was transformed into a BL21[DE3] E. coli host. The resulting recombinant E. coli strains were grown in 250 mL shake flask cultures containing 50 mL LB medium and antibiotic selection pressure at 37° C. with shaking at 230 rpm. Each culture was induced overnight at 16°C with 1 mM IPTG.

[0277] The pellet from each induced shake flask culture was harvested by centrifugation. Each pellet was resuspended and lysed by sonication. ...

Embodiment 2

[0283] Enzyme activity of carboxylic acid reductase using 6-hydroxyhexanoic acid as substrate and forming 6-hydroxyhexanal

[0284] The nucleotide sequence encoding the His-tag was added to the carboxylic acid reductases from Mycobacterium marinum, Mycobacterium smegmatis, Mycobacterium smegmatis, Segniliparus rugosus, Marseilles respectively encoding the carboxylic acid reductase of SEQ ID NO:3-7. Mycobacterium, and Segniliparus rotundus genes (see Figure 20 ), allowing the generation of an N-terminally HIS-tagged carboxylic acid reductase. Each modified gene was cloned into the pET Duet expression vector together with the sfp gene encoding the His-tagged phosphopantetheinyl transferase from Bacillus subtilis, all under the control of the T7 promoter. Each expression vector was transformed into a BL21[DE3] E. coli host. Each resulting recombinant E. coli strain was grown in a 250 mL shake flask culture containing 50 mL LB medium and antibiotic selection pressure at 37°C wi...

Embodiment 3

[0289] For 6-aminohexanol, omega-transaminase activity to form 6-oxohexanol

[0290] The nucleotide sequence encoding the N-terminal His-tag was added to Chromobacterium violaceum, Pseudomonas aeruginosa, Pseudomonas syringae, Rhodobacter sphaericus, Escherichia coli Bacillus and Vibrio genes (see Figure 20 ), allowing the generation of N-terminally HIS-tagged ω-transaminases. The modified gene was cloned into the pET21a expression vector under the T7 promoter. Each expression vector was transformed into a BL21[DE3] E. coli host. Each of the resulting recombinant E. coli strains was cultured in a 250 mL shake flask containing 50 mL of LB medium and antibiotic selection pressure at 37° C. with shaking at 230 rpm. Each culture was induced overnight at 16°C with 1 mM IPTG.

[0291] The pellet from each induced shake flask culture was harvested by centrifugation. Each pellet was resuspended and lysed by sonication. Cell debris was separated from the supernatant by centrifug...

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Abstract

The 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.

Description

[0001] Cross References to Related Applications [0002] This application claims priority to US Provisional Application Serial No. 61 / 993,532, filed May 15, 2015, the disclosure of which is hereby incorporated by reference in its entirety. [0003] field of invention [0004] Disclosed herein is the use of one of a polypeptide having 2-hydroxyacyl-CoA dehydratase activity, a polypeptide having mutase activity, a polypeptide having ammonia lyase activity, and a polypeptide having enoate reductase activity in a recombinant host or a plurality of methods for the biosynthesis of 2-aminopimelic acid from 2,6-diaminopimelic acid. Biosynthetic 2-aminopimelic acid can be enzymatically converted to a product selected from the group consisting of adipate, adipate semialdehyde, 6-aminocaproic acid, 6-hydroxycaproic acid, caprolactam, hexaethylene Methyldiamine and 1,6-hexanediol using e.g. polypeptides having alpha-ketoacid decarboxylase activity classified under EC 4.1.1.-, having One ...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C12P13/04
CPCC12P13/04C12N15/52C12Y402/01C12N9/001C12Y103/01031C12N9/88C12Y403/01C12N9/0008C12N9/1096C12Y102/99006C12P13/005C12P7/42C12P13/001
Inventor A.L.博特斯A.V.E.康拉迪
Owner INVISTA TEXTILES (U K) LTD
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