IP Library Granted Patent US 8,877,476
Granted Patent B2
US 8,877,476 · App. 13/700,507 · Granted Nov 4, 2014

Soluble and stable human 5-lipoxygenase

Inventors: Marcia E. Newcomer (Baton Rouge, LA); Sue G. Bartlett (Baton Rouge, LA); Nathaniel C. Gilbert (Nashville, TN)
Assignee: Board of Supervisors of Louisiana State University and Agricultural and Mechanical College
C12N9/0069C12Y113/11034C12Q1/26G01N2500/00
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Quick Facts
Patent No.
US 8,877,476
App. No.
13/700,507
Granted
Nov 4, 2014
Kind
B2
Abstract

A soluble and stable form of 5-lipoxygenase (5-LOX) has been made, 5-Lox is the enzyme which initiates leukotriene biosynthesis by catalyzing the two-step transformation of arachidomc acid to leukotriene A4 (LTA4). The soluble and stable 5-LOX is suitable for a number of applications, including, but not limited to, high throughput screening of 5-LOX inhibitors, structural analysis of the enzyme's active site, designing inhibitors based on the three-dimensional structure of the enzyme's active site, and synthesis of LTA4. Using Stable-5-LOX, the crystal structure for 5-LOX has been resolved and the amino acids defining the active site determined.

Claims (27)

1. An isolated 5-Lipoxygenase polypeptide comprising an amino acid sequence, numbered from the N-terminus, as set forth in SEQ ID NO: 1 with one or more of the following modifications selected from the group consisting of:

(a) a replacement of amino acids Tryptophan and Phenylalanine at residues 13-14 with Glutamic acid and Histidine, respectively;

(b) a replacement of amino acids Proline, Phenylalanine, Tyrosine, Asparagine and Aspartic Acid at residues 40-44 with Glycine-Serine;

(c) a replacement of amino acids Tryptophan and Leucine at residues 75-76 with Glycine and Serine, respectively;

(d) a replacement of amino acid Cysteine at residue 240 with Alanine;

(e) a replacement of amino acid Cysteine at residue 561 with Alanine; and

(f) a replacement of amino acids Lysine, Lysine and Lysine at residues 653-655 with Glutamic acid, Asparagine, and a non-positively charged amino acid, respectively.

2. The isolated 5-Lipoxygenase polypeptide of claim 1 , wherein the polypeptide further comprises an amino terminus sequence that includes a multiple histidine sequence.

3. The isolated 5-Lipoxygenase polypeptide of claim 1 , wherein the polypeptide further comprises a replacement of amino acid Serine at residue 663 with Aspartic Acid.

4. An isolated, soluble 5-Lipoxygenase polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 3 and SEQ ID NO: 4.

5. An isolated, stable 5-Lipoxygenase (5-LOX) polypeptide comprising an amino acid sequence, numbered from the N-terminus, as set forth in SEQ ID NO: 1 with a replacement of amino acids Lysine, Lysine and Lysine at residues 653-655 with Glutamic acid, Asparagine, and a non-positively charged amino acid, respectively.

6. An isolated, stable 5-Lipoxygenase (5-LOX) polypeptide comprising an amino acid sequence, numbered from the N-terminus, as set forth in SEQ ID NO: 1 with a replacement of amino acid Lysine at residue 655 with an amino acid having a non-positive charge.

7. An isolated, soluble and stable 5-Lipoxygenase polypeptide comprising an amino acid sequence, numbered from the N-terminus, as set forth in SEQ ID NO: 1 with the following modifications:

(a) a replacement of amino acids 13-14 with Glutamic acid and Histidine, respectively;

(b) a replacement of amino acids 40-44 with Glycine-Serine;

(c) a replacement of amino acids 75-76 with Glycine and Serine, respectively;

(d) a replacement of amino acid 240 with Alanine;

(e) a replacement of amino acid 561 with Alanine; and

(f) a replacement of amino acids 653-655 with Glutamic acid, Asparagine, and Leucine, respectively.

8. A crystalline 5-lipoxygenase comprising the amino acid sequence as set forth in SEQ ID NO: 3 or SEQ ID NO: 4, wherein said crystalline 5-lipoxygenase has space group P2 1 , and unit cell dimensions a=55.17 ű0.003 Å, b=202.89 ű0.003 Å, c=76.80 ű0.003 Å, and b=109.56°±0.714°.

9. An isolated nucleic acid molecule encoding the 5-Lipoxygenase polypeptide according to claim 1 .

10. An isolated nucleic acid molecule encoding the 5-Lipoxygenase polypeptide according to claim 2 .

11. An isolated nucleic acid molecule encoding the 5-Lipoxygenase polypeptide according to claim 3 .

12. An isolated nucleic acid molecule encoding the 5-Lipoxygenase polypeptide according to claim 4 .

13. An isolated nucleic acid molecule encoding the 5-Lipoxygenase polypeptide according to claim 5 .

14. An isolated nucleic acid molecule encoding the 5-Lipoxygenase polypeptide according to claim 6 .

15. An isolated nucleic acid molecule encoding the 5-Lipoxygenase polypeptide according to claim 7 .

Assignments (2)
CONFIRMATORY LICENSE Recorded Jan 7, 2015
From: LOUISIANA STATE UNIV A&M COL BATON ROUGE
To: NATIONAL SCIENCE FOUNDATION
Reel/Frame 034730/0789 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 27, 2013
From: NEWCOMER, MARCIA E.; BARTLETT, SUE G.; GILBERT, NATHANIEL C.
To: BOARD OF SUPERVISORS OF LOUISIANA STATE UNIVERSITY AND AGRICULTURAL AND MECHANICAL COLLEGE
Reel/Frame 029887/0632 →
Continuity (2)
Provisional Application 61350197 · Jun 1, 2010
Related Publication 20130210052A1 · Aug 15, 2013