A mutation interfering with 5-lipoxygenase domain interaction leads to increased enzyme activity

Archives of Biochemistry and Biophysics

Volumn 545, Issue , 2014, Pages 179-185

  Rakonjac Ryge, Marija ^a   Tanabe, Michiharu ^a,b   Provost, Patrick ^c,d   Persson, Bengt ^e   Chen, Xinsheng ^f   Funk, Colin D ^f,g   Rinaldo Matthis, Agnes ^a   Hofmann, Bettina ^h   Steinhilber, Dieter ^h   Watanabe, Takashi ^b   Samuelsson, Bengt ^a   Rådmark, Olof ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b TOTTORI UNIVERSITY   (Japan)

^c University Laval   (Canada)

^d UNIVERSITÉ LAVAL   (Canada)

^e UPPSALA UNIVERSITY   (Sweden)

^f UNIVERSITY OF PENNSYLVANIA   (United States)

^g QUEEN S UNIVERSITY   (Canada)

^h GOETHE UNIVERSITY   (Germany)

Author keywords

Arachidonic acid; Domain interaction; Eicosanoid; Leukotriene; Two hybrid system

Indexed keywords

ARACHIDONIC ACID; DOMAIN INTERACTION; EICOSANOID; LEUKOTRIENE; TWO-HYBRID SYSTEM;

AMINO ACID SEQUENCE; ARACHIDONATE 5-LIPOXYGENASE; CATALYTIC DOMAIN; ENZYME ACTIVATION; HUMANS; LEUKOTRIENES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN STRUCTURE, TERTIARY;

EID: 84894257223     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2014.01.017     Document Type: Article

References (40)

1. B. Samuelsson Science 220 4597 1983 568 575
2. J.Z. Haeggstrom, and C.D. Funk Chem. Rev. 111 10 2011 5866 5898
3. V.C. Tam et al. Cell 154 1 2013 213 227
4. D. Wang, and R.N. Dubois Nat. Rev. Cancer 10 3 2010 181 193
5. N.C. Gilbert et al. Science 331 6014 2011 217 219
6. J.B. Allard, and T.G. Brock Curr. Protein Pept. Sci. 6 2 2005 125 131
7. O. Radmark, and B. Samuelsson Biochem. Biophys. Res. Commun. 396 1 2010 105 110
8. M. Rakonjac et al. Proc. Natl. Acad. Sci. USA 103 35 2006 13150 13155
9. J. Esser et al. Biochem. J. 425 1 2009 265 274
10. A.K. Hafner et al. Biol. Chem. 392 12 2011 1097 1111
11. A.K. Mandal et al. Proc. Natl. Acad. Sci. USA 105 51 2008 20434 20439
12. A.M. Bair et al. Mol. Biol. Cell 23 22 2012 4456 4464
13. O. Werz, and D. Steinhilber Biochem. Pharmacol. 70 3 2005 327 333
14. M. Luo et al. J. Biol. Chem. 280 49 2005 40609 40616
15. C. Pergola et al. Proc. Natl. Acad. Sci. USA 105 50 2008 19881 19886
16. E. Buerkert et al. J. Biol. Chem. 278 44 2003 42846 42853
17. P. Provost et al. Proc. Natl. Acad. Sci. USA 96 5 1999 1881 1885
18. P. Eek et al. J. Biol. Chem. 287 26 2012 22377 22386
19. T. Watanabe et al. Eur. J. Biochem. 212 2 1993 605 612
20. P. James et al. Genetics 144 1996 1425 1436
21. Y.Y. Zhang et al. Biochem. J. 351 Pt 3 2000 697 707
22. T. Hammarberg et al. J. Biol. Chem. 275 49 2000 38787 38793
23. P. Provost et al. J. Biol. Chem. 276 19 2001 16520 16527
24. X.S. Chen, and C.D. Funk J. Biol. Chem. 276 1 2001 811 818
25. X.S. Chen et al. Eur. J. Biochem. 214 3 1993 845 852
26. T. Izumi et al. Proc. Natl. Acad. Sci. USA 87 19 1990 7477 7481
27. K.V. Reddy et al. Biochemistry 39 7 2000 1840 1848
28. S. Kulkarni et al. J. Biol. Chem. 277 15 2002 13167 13174
29. M. Walther et al. Arch. Biochem. Biophys. 516 1 2011 1 9
30. M. Walther et al. J. Biol. Chem. 277 30 2002 27360 27366
31. T. Hammarberg et al. Eur. J. Biochem. 230 2 1995 401 407
32. W. Minor et al. Biochemistry 35 33 1996 10687 10701
33. S.A. Gillmor et al. Nat. Struct. Biol. 4 12 1997 1003 1009
34. J. Choi et al. Proteins 70 3 2008 1023 1032
35. M. Hammel et al. J. Mol. Biol. 343 4 2004 917 929
36. I. Ivanov et al. Biochim. Biophys. Acta 1811 12 2011 1001 1010
37. M.L. Oldham et al. J. Biol. Chem. 280 47 2005 39545 39552
38. C. Palmieri-Thiers et al. Arch. Biochem. Biophys. 509 1 2011 82 89
39. J. Saam et al. Proc. Natl. Acad. Sci. USA 104 33 2007 13319 13324
40. F. Pietra Chem. Biodivers. 9 6 2012 1019 1032