Bioconversion process for producing nylon-7, nylon-7,7 and polyesters

Patent metadata

Field	Value
Publication number	US-9650653-B2
Application number	US-201214130117-A
Country	US
Kind code	B2
Filing date	Jun 29, 2012
Priority date	Jun 30, 2011
Publication date	May 16, 2017
Grant date	May 16, 2017

Abstract

Embodiments of the present invention relate to methods for the biosynthesis of di- or trifunctional C7 alkanes in the presence of isolated enzymes or in the presence of a recombinant host cell expressing those enzymes. The di- or trifunctional C7 alkanes are useful as intermediates in the production of nylon-7, nylon-7,x, nylon-x,7, and polyesters.

First claim

We claim:

1. A method of converting a compound, the method comprising (a) contacting pimeloyl acyl carrier protein (PACP) with an enzyme that catalyzes the thioester hydrolysis of PACP to pimelic acid (PA), wherein PA is produced, and
(b) further contacting the PA with an enzyme that catalyzes the carboxylic acid reduction of PA to pimelic acid semialdehyde (PAS), wherein PAS is produced.

2. The method of claim 1 , wherein the enzyme that catalyzes the thioester hydrolysis of PACP to PA is a thioesterase, an acid-thiol ligase, or a CoA transferase.

3. The method of claim 2 , wherein:
the thioesterase is a thioesterase in EC 3.1.2;
the acid-thiol ligase is an acid-thiol ligase in EC 6.2.1, and
the CoA transferase is a CoA transferase in EC 2.8.3.

4. The method of claim 3 , wherein:
the thioesterase in EC 3.1.2 is one more of
the thioesterase in EC 3.1.2.18, EC 3.1.2.19, or EC 3.1.2.20,
the gene product of yciA,
a thioesterase in EC 3.1.2.14, and
the gene product of fatA or fatB;

the acid-thiol ligase in EC 6.2,1 is
an acid-thiol ligase in EC 6.2,1,14, or EC 6.2.1.23; and

the CoA transferase in EC 2.8.3 is
a CoA transferase in EC 2.8.3.12, EC 2.8.3.13, or EC 2.8.3.14.

5. The method of claim 1 , wherein the PACP is produced by a process comprising one or more steps of
the biotin biosynthesis pathway I (see FIG. 6 ).

6. The method of claim 1 , wherein the enzyme that catalyzes the carboxylic acid reduction of PA to PAS is one or more of
a carboxylic acid reductase, and
a carboxylic acid reductase in EC 1.2.99.

7. The method of claim 6 , wherein the carboxylic acid reductase in EC 1.2.99 is a carboxylic acid reductase in EC 1.2.99.6.

8. The method of claim 1 , the method further comprising contacting PACP with an enzyme that catalyzes the reduction of PACP to PAS, wherein PAS is produced.

9. The method of claim 8 , wherein the enzyme that catalyzes the reduction of PACP to PAS is one or more of
a fatty-acyl-CoA reductase or an aldehyde dehydrogenase;
a fatty-acyl-CoA reductase or an aldehyde dehydrogenase is a reductase in EC 1.2.1,
a fatty-acyl-CoA reductase or aldehyde dehydrogenase in EC 1.2.1.4, EC 1.2.1.50, EC 1.2.1.83, or EC 1.2.1.80.

10. The method of claim 8 , wherein the PACP is produced by a process comprising one or more steps of:
the biotin biosynthesis pathway I (see FIG. 6 ).

11. The method of claim 8 , wherein the enzyme, or one or more enzymes, is or are:
(i) isolated; (ii) in cell lysate, a partially purified cell lysate, cell lysates, or partially purified cell lysates; or (iii) in one or more host cell strains recombinantly expressing it or them.

12. The method of claim 1 , the method further comprising contacting α-ketosuberate (AKS) with an enzyme that catalyzes the α-keto decarboxylation of AKA to PAS, wherein PAS is produced.

13. The method of claim 12 , wherein the enzyme that catalyzes the α-keto decarboxylation of AKS to PAS is one or more of
a decarboxylase or an acetolactate synthase, and
an enzyme in EC.4.1.1.

14. The method of claim 13 , wherein the AKS is produced by a process comprising one or more steps of:
(a) a pathway shown in FIG. 10 ; or
(b) the coenzyme B pathway of methanogenic archae (see FIG. 3 ).

15. The method of claim 12 , wherein the AKS is produced by a process comprising one or more steps of:
(a) a pathway shown in FIG. 10 ; or
(b) the coenzyme B pathway of methanogenic archae (see FIG. 3 ).

16. The method of claim 12 , wherein the enzyme, or one or more enzymes, is or are:
(i) isolated; (ii) in a cell lysate or partially purified cell lysate; or (iii) in a host cell recombinantly expressing it or them.

17. The method of claim 1 , the method further comprising contacting AKS with an enzyme that catalyzes the transfer of an amino group to the AKS to produce α-amino suberate (AAS), wherein AAS is produced.

18. The method of claim 17 , wherein the enzyme that catalyzes the transfer of an amino group to the AKS to produce α-amino suberate (AAS) is one or more of
an amino acid aminotransferase,
an aminotransferase in EC 2.6.1, or
an amino acid aminotransferase in EC 2.6.1.39, EC 2.6.1.42, or EC 2.6.1.67.

19. The method of claim 17 , further comprising contacting the AAS with an enzyme that catalyzes the α-amino acid decarboxylation of the AAS to 7-amino-heptanoic acid (7 AHA), wherein 7 AHA is produced.

20. The method of claim 19 , wherein the enzyme that catalyzes the α-amino acid decarboxylation of the AAS to 7-amino-heptanoic acid (7 AHA) is one or more of
a decarboxylase or an acetolactate synthase, or
an enzyme in EC.4.1.1.

21. The method of claim 19 , further comprising contacting the 7 AHA with an enzyme that catalyzes the amide hydrolysis of the 7 AHA to enantholactam (ENTL), wherein ENTL is produced.

22. The method of claim 19 , further comprising contacting the 7 AHA with an enzyme that catalyzes the aldehyde dehydrogenation of the 7 AHA to 7-amino-heptanal (7 AHT), wherein 7 AHT is produced.

23. The method of claim 22 , further comprising contacting the 7 AHT with an enzyme that catalyzes the transfer of an amino group to the 7 AHT to produce 1,7-diaminoheptane (1,7 DAH), wherein 1,7 DAH is produced.

24. The method of claim 17 , wherein the enzyme, or one or more enzymes, is or are:
(i) isolated; (ii) in a cell lysate or partially purified cell lysate; or (iii) in a host cell recombinantly expressing it or them.

25. The method of claim 1 , the method further comprising contacting PAS with an enzyme that catalyzes the semialdehyde amination of the PAS to 7-amino-heptanoic acid (7 AHA), wherein 7 AHA is produced.

26. The method of claim 25 , further comprising contacting the 7 AHA with an enzyme that catalyzes the amide hydrolysis of the 7 AHA to enantholactam (ENTL), wherein ENTL is produced.

27. The method of claim 25 , further comprising:
contacting the 7 AHA with an enzyme that catalyzes the aldehyde dehydrogenation of the 7 AHA to 7-amino-heptanal (7 AHT), wherein AHT is produced; and
contacting the 7 AHT with an enzyme that catalyzes the transfer of an amino group to the 7 AHT to produce 1,7-diaminoheptane (1,7 DAH), wherein 1,7 DAH is produced.

28. The method of claim 25 , wherein the PAS is produced by a process comprising:
(1) contacting a-ketosuberate (AKS) with an enzyme that catalyzes the α-keto decarboxylation of AKS to PAS; or
(2) one or more steps of the Tetralin degradation pathway (see FIG. 8 ).

29. The method of claim 25 , wherein the enzyme, or one or more enzymes, is or are:
(i) isolated; (ii) in a cell lysate or partially purified cell lysate; or (iii) in a host cell recombinantly expressing it or them.

30. The method of claim 1 , the method further comprising contacting 7 AHT with an enzyme that catalyzes the transfer of an amino group to the 7 AHT to produce 1,7-diaminoheptane (1,7 DAH), wherein 1,7 DAH is produced.

31. The method of claim 30 , wherein the enzyme that catalyzes the transfer of an amino group to the 7 AHT to produce 1,7-diaminoheptane (1,7 DAH) is one or more of
an amino acid aminotransferase or an ω-transaminase,
an amino acid aminotransferase in EC 2.6.1 or an ω-transaminase in EC.2.6.1,
an amino acid aminotransferase in EC 2.6.1.39, EC 2.6.1.42, or EC 2.6.1.67, and
an ω-transaminase in EC 2.6.1.18, EC 2.6.1.19, or EC 2

Assignees

• Pearlman Paul S
• Chen Changlin
• Botes Adriana L
• Conradie Alex Van Eck
• Herzog Benjamin D
• Invista North America Sarl

Inventors

• Pearlman Paul S
• Chen Changlin
• Botes Adriana L
• Conradie Alex Van Eck
• Herzog Benjamin D

Classifications

• C12P13/02

  Amides, e.g. chloramphenicol {or polyamides; Imides or polyimides; Urethanes, i.e. compounds comprising N-C=O structural element or polyurethanes (peptides C12P21/00 or C07K)} · CPC title

• C12Y301/02018

  ADP-dependent short-chain-acyl-CoA hydrolase (3.1.2.18) · CPC title

• C12N9/1096

  transferring nitrogenous groups (2.6) · CPC title

• C12P13/005

  Amino acids other than alpha- or beta amino acids, e.g. gamma amino acids · CPC title

• C12N9/1025

  Acyltransferases (2.3) · CPC title