IP Library Granted Patent US 8,530,213
Granted Patent B2
US 8,530,213 · App. 12/958,949 · Granted Sep 10, 2013

Compositions and methods for using NADH oxidases

Inventors: Andreas Bommarius (Atlanta, GA); Bettina Bommarius (Atlanta, GA); Jun-Ichiro Hirano (Atlanta, GA); Vaijayanthi Thangavel (Atlanta, GA); Jonathan Taejoo Park (Atlanta, GA)
Assignees: Georgia Tech Research Corporation; Emory University
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Quick Facts
Patent No.
US 8,530,213
App. No.
12/958,949
Granted
Sep 10, 2013
Kind
B2
Abstract

The present disclosure relates generally to bacterial NADH oxidases and, more particularly, to novel NADH oxidases obtained from Lactobacillus plantarum , and derivatives thereof that demonstrate enzymatic activity for NADH, NADPH, or both NADH and NADPH. The compositions comprising an NADH oxidase obtained from L. plantarum or derivatives thereof include: isolated enzymes; recombinantly produced enzymes and derivatives thereof, as well as catalytically active portions thereof; nucleic acids encoding an NADH oxidase obtained from L. plantarum , derivatives thereof, and portions thereof. The methods of the present invention include isolation of NADH oxidases obtained from L. plantarum , derivatives thereof, and portions thereof, and methods for enzymatic reactions comprising NADH oxidase obtained from L. plantarum , including the production of enantiomer-enriched organic compounds.

Claims (18)

1. An isolated bacterial NADH oxidase, which is obtained from Lactobacillus plantarum , and regenerates NADP+ and NAD+, comprising

at least one amino acid mutation that facilitates enzymatic activity towards NADPH and comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, and SEQ ID NO: 17.

2. The isolated bacterial NADH oxidase of claim 1 , encoded by a nucleic acid sequence, which hybridizes under stringent conditions to the nucleic acid selected from the group consisting of SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 10, SEQ ID NO: 13, and SEQ ID NO: 18.

3. The isolated bacterial NADH oxidase of claim 1 , which comprises SEQ ID NO: 8.

4. The isolated bacterial NADH oxidase of claim 3 , encoded by a nucleic acid sequence comprising SEQ ID NO: 10.

5. The isolated bacterial NADH oxidase of claim 1 , which comprises SEQ ID NO: 16.

6. The isolated bacterial NADH oxidase of claim 5 , encoded by a nucleic acid sequence comprising SEQ ID NO: 18.

7. A method of producing an enantiomer-enriched organic compound, comprising:

reacting a substrate with a first enzyme selective for producing an enantiomer, wherein the first enzyme requires a oxidized nicotinamide-based cofactor for catalytic activity;

producing the enantiomer, its oxidized counterpart, and a reduced nicotinamide-based cofactor; and

oxidizing the reduced nicotinamide-based cofactor with a second enzyme selective for a nicotinamide-based cofactor,

wherein the second enzyme selective for a nicotinamide-based cofactor comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, or SEQ ID NO: 17.

8. The method of producing an enantiomer-enriched organic compound of claim 7 , wherein the enantiomer comprises an L-nucleoside, and wherein the second enzyme selective for a nicotinamide-based cofactor comprises a NADH oxidase obtained from Lactobacillus plantarum.

9. The method of producing an enantiomer-enriched organic compound of claim 7 , wherein the second enzyme selective for a nicotinamide-based cofactor can oxidize NADPH and NADH.

10. The method of producing an enantiomer-enriched organic compound of claim 9 , wherein the second enzyme selective for a nicotinamide-based cofactor comprises SEQ ID NO: 8.

11. The method of producing an enantiomer-enriched organic compound of claim 9 , wherein the second enzyme selective for a nicotinamide-based cofactor comprises SEQ ID NO: 18.

12. The method of producing an enantiomer-enriched organic compound of claim 7 , wherein the second enzyme selective for a nicotinamide-based cofactor can catalyze more than 113,000 turnovers per active site.

13. The method of producing an enantiomer-enriched organic compound of claim 7 , wherein the second enzyme selective for a nicotinamide-based cofactor can catalyze more than 100,000 turnovers per active site in the absence of an externally added reducing agent.

Assignments (3)
CONFIRMATORY LICENSE Recorded Nov 7, 2013
From: GEORGIA TECH RESEARCH CORPORATION
To: NATIONAL INSTITUTES OF HEALTH (NIH), U.S. DEPT. OF HEALTH AND HUMAN SERVICES (DHHS), U.S. GOVERNMENT
Reel/Frame 031598/0445 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jul 7, 2011
From: BOMMARIUS, ANDREAS; HIRANO, JUN-ICHIRO; THANGAVEL, VAIJAYANTHI; PARK, JONATHAN TAEJOO
To: GEORGIA TECH RESEARCH CORPORATION
Reel/Frame 026554/0633 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jul 7, 2011
From: BOMMARIUS, BETTINA
To: EMORY UNIVERSITY
Reel/Frame 026554/0660 →
Continuity (3)
Provisional Application 61383858 · Sep 17, 2010
Provisional Application 61265915 · Dec 2, 2009
Related Publication 20120003688A1 · Jan 5, 2012