IP Library Granted Patent US 50,715
Granted Patent E1
US 50,715 · App. 18/052,136 · Granted Dec 30, 2025

Synthetic biochemistry molecular purge valve module that maintain co-factor balance

Inventors: James U. Bowie (Culver City, CA); Paul H. Opgenorth (Los Angeles, CA); Tyler P. Korman (Sierra Madre, CA)
Assignee: The Regents of the Univesity of California
C12P5/007C12N9/0008C12N9/1029C12P7/625C12Y102/01051C12Y106/99001C12Y108/01004C12Y203/01012
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 50,715
App. No.
18/052,136
Granted
Dec 30, 2025
Kind
E1
Abstract

The disclosure provides a metabolic pathway for producing a metabolite, the metabolic pathway having a co-factor purge valve system for recycling a cofactor used in the metabolic pathway.

Claims (24)

1 . A recombinant, artificial or engineered metabolic pathway comprising a plurality of enzymatic steps that converts a substrate to a product, wherein the pathway produces an unbalanced production of a cofactor cofactors, said pathway comprising:

a first cofactor-dependent enzyme that is capable of converting a first substrate to a second substrate, said first cofactor-dependent enzyme producing the unbalanced production of a first cofactor; and

a second cofactor-dependent enzyme comprising that uses a second cofactor different from the first cofactor-dependent enzyme and that converts the first substrate to the second substrate and wherein said second cofactor-dependent enzyme produces an unbalanced production of the second cofactor, and wherein the pathway comprises an NADH or an NADPH oxidase that recycles the an NADH or NADPH cofactor.

2 . The recombinant, artificial or engineered pathway of claim 1 , wherein the first and second co-factor is an co-factors are oxidizing/reducing co-factor co-factors.

3 . The recombinant, artificial or engineered pathway of claim 2 , wherein the oxidizing/reducing co-factor is co-factors are selected from the group consisting of NAD + /NADH, NADP + /NADPH and FAD + /FADH.

4 . The recombinant, artificial or engineered pathway of claim 1 , wherein the cofactor first and second cofactors comprises NAD + /NADH or and NADP + /NADPH.

5 . The recombinant, artificial or engineered pathway of claim 1 , wherein the first cofactor-dependent enzyme comprises an NADH or an NADPH dehydrogenase.

6 . The recombinant, artificial or engineered pathway of claim 5 , wherein the NADH dehydrogenase is a NADH pyruvate dehydrogenase complex.

7 . The recombinant, artificial or engineered pathway of claim 6 , wherein the NADH pyruvate dehydrogenase complex comprises a pyruvate dehydrogenase subunit a, a pyruvate dehydrogenase subunit b, a dihydrolipoamide acetyltransferase, and a dihydrolipoamide dehydrogenase.

8 . The recombinant, artificial or engineered pathway of claim 7 , wherein the pyruvate dehydrogenase subunit a comprises a sequence that has at least 90% sequence identity to SEQ ID NO: 1, wherein the pyruvate dehydrogenase subunit b comprises a sequence that has at least 90% sequence identity to SEQ ID NO: 2, wherein the dihydrolipoamide acetyltransferase has at least 90% sequence identity to SEQ ID NO: 3, and wherein the dihydrolipoamide dehydrogenase has at least 90% sequence identity to SEQ ID NO: 5, wherein the complex converts pyruvate to acetyl-CoA.

9 . The recombinant, artificial or engineered pathway of claim 7 , wherein the pyruvate dehydrogenase subunit a comprises a sequence that has at least 90% sequence identity to SEQ ID NO: 1, wherein the pyruvate dehydrogenase subunit b comprises a sequence that has at least 90% sequence identity to SEQ ID NO: 2, wherein the dihydrolipoamide acetyltransferase has at least 90% sequence identity to SEQ ID NO: 3, and wherein the dihydrolipoamide dehydrogenase has at least 90% sequence identity to SEQ ID NO: 7 and preferentially uses NADP + , wherein the complex converts pyruvate to acetyl-CoA.

10 . The recombinant, artificial or engineered pathway of claim 5 , wherein the NADPH dehydrogenase is a member of a NADPH pyruvate dehydrogenase complex.

11 . The recombinant, artificial or engineered pathway of claim 10 , wherein the NADPH pyruvate dehydrogenase complex comprises a pyruvate dehydrogenase subunit a, a pyruvate dehydrogenase subunit b, a dihydrolipoamide acetyltransferase, and a mutant dihydrolipoamide dehydrogenase the that preferentially uses NADP + .

12 . The recombinant, artificial or engineered pathway of claim 1 , wherein the NADH or the NADPH oxidase is a NoxE or homolog thereof.

13 . The recombinant, artificial or engineered pathway of claim 12 , wherein the NADH or the NADPH oxidase comprises a sequence that has at least 50% sequence identity to SEQ ID NO: 10.

14 . The recombinant, artificial or engineered pathway of claim 1 , wherein the pathway is in a cell-free system.

15 . The recombinant, artificial or engineered pathway of claim 1 , wherein the pathway is in a living cell.

16 . The recombinant, artificial or engineered pathway of claim 1 , wherein the recombinant, artificial or engineered pathway produces PHB.

17 . The recombinant, artificial or engineered pathway of claim 1 , wherein the recombinant, artificial or engineered pathway produces ethanol.

18 . The recombinant, artificial or engineered pathway of claim 1 , wherein the recombinant, artificial or engineered pathway produces lactate.

19 . An enzymatic system comprising a metabolic pathway including a plurality of enzymes for converting a substrate to a product, the metabolic pathway having an unbalanced utilization of reducing/oxidizing cofactors, wherein the enzymatic system comprises

a first cofactor-dependent enzyme that is capable of converting the substrate to the product, said first cofactor-dependent enzyme producing the unbalanced production of a first cofactor; and

a second cofactor-dependent enzyme that uses a second cofactor than the first cofactor-dependent enzyme and that converts the substrate to the product and wherein said second cofactor-dependent enzyme produces an unbalanced production of the second cofactor, and a metabolic purge valve comprising an NADH pyruvate dehydrogenase and a NADH/NADPH an NADH or an NADPH oxidase.

20 . A recombinant polypeptide comprising a sequence that has at least 99% sequence identity to SEQ ID NO: 5 and comprising the mutations E206V, G207R, A208K, and S213R, wherein the polypeptide has dihydrolipoamide dehydrogenase activity.

Assignments (1)
CONFIRMATORY LICENSE Recorded Sep 9, 2026
From: UCLA TECHNOLOGY DEVELOPMENT GROUP
To: UNITED STATES GOVERNMENT
Reel/Frame 075956/0333 →
Continuity (3)
Continuation 15127351
Provisional Application 61974311 · Apr 2, 2014
Reissue 16243332 · Jan 9, 2019
References Cited (25)
US 10196653B2 · Bowie · 2019 [cited by examiner]
US 20050048596A1 · Kristian · 2005 [cited by examiner]
US 20130030164A1 · Yoshida · 2013 [cited by examiner]
US 20140058056A1 · Burgard et al. · 2014 [cited by applicant]
US 20140342419A1 · Dischert · 2014 [cited by examiner]
US 20140377798A1 · Ertl · 2014 [cited by examiner]
WO 2010051527A2 · 2010 [cited by applicant]
Lopez de Felipe, F., et al. J. Bacteriol. (1998), 180(15); 3804-3808. [cited by examiner]
Hawkins, C. F., et al. Eur. J. Biochem (1990), 191; 337-346. [cited by examiner]
Merriam-Webster's Cllegiate Dictionary (2002), Tenth Edition; “unbalanced” definition. [cited by examiner]
Berrios-Rivera et al., “Metabolic engineering of [cited by applicant]
Bologna et al., “ [cited by applicant]
Heux et al., “Cofactor engineering in [cited by applicant]
Nickitas-Etienne, International Preliminary Report on Patentability and Written Opinion, PCT/US2015/024181, The International Bureau of WIPO, Oct. 13, 2016. [cited by applicant]
Niebuhr-Ebel, K., Extended European Search Report, Application No. 15774454.1, European Patent Office, Jul. 17, 2017. [cited by applicant]
Niebuhr-Ebel, K., Extended European Search Report, European Patent Office, Application No. 19212269.5, Jan. 30, 2020. [cited by applicant]
Nikel et al., “Redox driven metabolic tuning”, Bioengineered Bugs, Jul. 1, 2010, 1(4), pp. 291-295. [cited by applicant]
Opgenorth et al., “A synthetic biochemistry molecular purge valve module that maintains redox balance,” Nat. Commun., Jun. 17, 2014, vol. 5, Article No. 4113, 8 pages. [cited by applicant]
Thomas, Shane, International Search Report and Written Opinion, PCT/US2015/024181, United States Patent and Trademark Office, Sep. 18, 2015. [cited by applicant]
Korman et al., “A synthetic biochemistry system for the in vitro production of isoprene from glycolysis intermediates”, Protein Science, 23:5, Mar. 12, 2014 (published online Feb. 6, 2014), pp. 576-585. [cited by applicant]
Satoh et al., “Enzyme-catalyzed poly(3-hydroxybutyrate) synthesis from acetate with CoA recycling and NADPH regeneration in vitro”, Journal of Bioscience of Bioengineering, 95:4, Jan. 1, 2003, pp. 335-341. [cited by applicant]
Korman Tyler P. et al., “A synthetic biochemistry platform for cell free production of monoterpenes from glucose”, Nature Communications, vol. 8, No. 1, Aug. 1, 2017, pp. 1-8. [cited by applicant]
Niebuhr-Ebel, K., Extended European Search Report, European Patent Office, Application No. 19212269.5, dated Jan. 30, 2020. [cited by applicant]
Opgenorth et al., “A synthetic biochemistry module for production of bio-based chemicals from glucose”, Nature Chemical Biology, vol. 12, No. 6, Jun. 1, 2016, pp. 393-395. [cited by applicant]
Opgenorth et al., “A molecular rheostate maintains ATP levels to drive a synthetic biochemistry system”, Nature Chemical Biology, vol. 13, No. 9, Sep. 1, 2017, pp. 938-942. [cited by applicant]