An active-site mutation enhances the catalytic activity of the yeast Cryptococcus humicola d-aspartate oxidase

Journal of Molecular Catalysis B: Enzymatic

Volumn 61, Issue 3-4, 2009, Pages 235-240

  Takahashi, Shouji ^a   Matsumoto, Shunske ^a   Maruyama, Kazuhiro ^a   Wakaizumi, Ayaka ^a   Abe, Katsumasa ^a   Kera, Yoshio ^a   Yamada, Ryo hei ^a  

^a NAGAOKA UNIVERSITY OF TECHNOLOGY   (Japan)

Author keywords

Cryptococcus humicola; d Aspartate oxidase; FAD enzyme; Site directed mutagenesis; Yeast

Indexed keywords

ARGININE RESIDUE; BINDING ABILITIES; CATALYTIC ACTIVITY; CATALYTIC EFFICIENCIES; CRYPTOCOCCUS HUMICOLA; D-AMINO ACID OXIDASE; D-ASPARTATE; FAD ENZYME; KINETIC ANALYSIS; SITE DIRECTED MUTAGENESIS; SPECTRAL FEATURE; SUBSTRATE RECOGNITION; SUBSTRATE SPECIFICITY; THREE-DIMENSIONAL MODEL; WILD TYPES; WILD-TYPE ENZYMES;

AMINES; AMINO ACIDS; CATALYST ACTIVITY; CHEMICAL INDUSTRY; CHEMICAL REACTIVITY; CRYSTAL STRUCTURE; ELECTROCHEMICAL SENSORS; ENZYMES; MUTAGENESIS; ORGANIC ACIDS; THREE DIMENSIONAL; YEAST;

SUBSTRATES;

ARGININE; ASPARTATE OXIDASE; ASPARTIC ACID; QUERCETIN;

ARTICLE; CONTROLLED STUDY; CRYPTOCOCCUS; CRYPTOCOCCUS HUMICOLA; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENE MUTATION; NONHUMAN; SITE DIRECTED MUTAGENESIS; THREE DIMENSIONAL IMAGING; WILD TYPE;

CRYPTOCOCCUS HUMICOLA;

EID: 72049104205     PISSN: 13811177     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcatb.2009.07.011     Document Type: Article

References (38)

1. Still J.L., Buell M.V., Knox W.E., and Green D.E. J. Biol. Chem. 179 (1949) 831-837
2. Negri A., Ceciliani F., Tedeschi G., Simonic T., and Ronchi S. J. Biol. Chem. 267 (1992) 11865-11871
3. Negri A., Massey V., and Williams Jr. C.H. J. Biol. Chem. 262 (1987) 10026-10034
4. Tedeschi G., Negri A., Ceciliani F., Ronchi S., Vetere A., D'Aniello G., and D'Aniello A. Biochim. Biophys. Acta 1207 (1994) 217-222
5. Wakayama M., Nakashima S., Sakai K., and Moriguchi M. J. Ferment. Bioeng. 78 (1994) 377-379
6. Yamada R., Ujiie H., Kera Y., Nakase T., Kitagawa K., Imasaka T., Arimoto K., Takahashi M., and Matsumura Y. Biochim. Biophys. Acta 1294 (1996) 153-158
7. Simonic T., Duga S., Negri A., Tedeschi G., Malcovati M., Tenchini M.L., and Ronchi S. Biochem. J. 322 (1997) 729-735
8. Setoyama C., and Miura R. J. Biochem. 121 (1997) 798-803
9. Takahashi S., Takahashi T., Kera Y., Matsunaga R., Shibuya H., and Yamada R.H. J. Biochem. 135 (2004) 533-540
10. Katane M., Furuchi T., Sekine M., and Homma H. Amino Acids 32 (2006) 69-78
11. D'Aniello A. Brain Res. Rev. 53 (2007) 215-234
12. Schell M.J., Cooper O.B., and Snyder S.H. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 2013-2018
13. Nagata Y., Homma H., Matsumoto M., and Imai K. FEBS Lett. 454 (1999) 317-320
14. D'Aniello A., Di Fiore M.M., Fisher G.H., Milone A., Seleni A., D'Aniello S., Perna A.F., and Ingrosso D. FASEB J. 14 (2000) 699-714
15. Wang H., Wolosker H., Pevsner J., Snyder S.H., and Selkoe D.J. J. Endocrinol. 167 (2000) 247-252
16. Wolosker H., D'Aniello A., and Snyder S.H. Neuroscience 100 (2000) 183-189
17. D'Aniello A., Spinelli P., De Simone A., D'Aniello S., Branno M., Aniello F., Fisher G.H., Di Fiore M.M., and Rastogi R.K. FEBS Lett. 552 (2003) 193-198
18. Homma H. Amino Acids 32 (2007) 3-11
19. Watanabe T., Shibata K., Kera Y., Takahashi S., and Yamada R. Amino Acids 28 (2005) 291-296
20. Fisher G.H., D'Aniello A., Vetere A., Padula L., Cusano G.P., and Man E.H. Brain Res. Bull. 26 (1991) 983-985
21. Konnno R., Bruckner H., D'Aniello A., Fisher G.H., Fujii N., and Homma H. d-Amino Acids (2006), Nova Science Publishers Inc., New York pp. 17-148
22. Sambrook J., and Russell D.W. Molecular Cloning: A Laboratory Manual. 3rd ed. (2001), Cold Spring Harbor Laboratory Press, New York pp. A2.2-A2.4
23. Tyagi R., Lai R., and Duggleby R.G. BMC Biotechnol. 4 (2004) 2
24. Lowry O.H., Rosebrough N.J., Farr A.L., and Randall R.J. J. Biol. Chem. 193 (1951) 265-275
25. Laemmli U.K. Nature 227 (1970) 68-685
26. Pollegioni L., Diederichs K., Molla G., Umhau S., Welte W., Ghisla S., and Pilone M.S. J. Mol. Biol. 324 (2002) 535-546
27. Sacchi S., Lorenzi S., Molla G., Pilone M.S., Rossetti C., and Pollegioni L. J. Biol. Chem. 277 (2002) 27510-27516
28. Mizutani H., Miyahara I., Hirotsu K., Nishina Y., Shiga K., Setoyama C., and Miura R. J. Biochem. (Tokyo) 120 (1996) 14-17
29. Mattevi A., Vanoni M.A., Todone F., Rizzi M., Teplyakov A., Coda A., Bolognesi M., and Curti B. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 7496-7501
30. Todone F., Vanoni M.A., Mozzarelli A., Bolognesi M., Coda A., Curti B., and Mattevi A. Biochemistry 36 (1997) 5853-5860
31. Miura R., Setoyama C., Nishina Y., Shiga K., Mizutani H., Miyahara I., and Hirotsu K. J. Biochem. 122 (1997) 825-833
32. Setoyama C., Nishina Y., Mizutani H., Miyahara I., Hirotsu K., Kamiya N., Shiga K., and Miura R. J. Biochem. 139 (2006) 873-879
33. Massey V., and Palmer G. Biochemistry 5 (1966) 3181-3189
34. Katane M., Hanai T., Furuchi T., Sekine M., and Homma H. Amino Acids 35 (2008) 75-82
35. Coulombe R., Yue K.Q., Ghisla S., and Vrielink A. J. Biol. Chem. 276 (2001) 30435-30441
36. Kuwabara Y., Nishino T., Okamoto K., Matsumura T., Eger B.T., Pai E.F., and Nishino T. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 8170-8175
37. Yamamoto A., Tanaka H., Ishida T., and Horiike K. J. Biochem. 141 (2007) 363-376
38. Negri A., Massey V., Williams Jr. C.H., and Schopfer L.M. J. Biol. Chem. 263 (1988) 13557-13563