Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha

Biochemistry

Volumn 45, Issue 10, 2006, Pages 3178-3188

  DuBois, Jennifer L ^a,b   Klinman, Judith P ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF NOTRE DAME   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDES; AMINES; AMINO ACIDS; COPPER; MUTAGENESIS; OXIDATION; YEAST;

ACTIVE SITE TYROSINE; COFACTOR GENESIS; HANSENULA POLYMORPHA; TOPAQUINONE (TPQ) FACTOR;

ENZYMES;

ALDEHYDE DERIVATIVE; AMINE; AMINE OXIDASE (COPPER CONTAINING); AMINO ACID; BENZYLAMINE; BUFFER; COPPER; ETHYLAMINE; OXYGEN; PEROXIDE; QUINONE DERIVATIVE; REAGENT; REDUCING AGENT; TOPAQUINONE COFACTOR; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; COLORIMETRY; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE; HANSENULA POLYMORPHA; HIGH TEMPERATURE; MUTANT; MUTATION; NONHUMAN; OXIDATION; PH; PRIORITY JOURNAL; SPECTRAL SENSITIVITY; STORAGE; WILD TYPE;

AMINE OXIDASE (COPPER-CONTAINING); BINDING SITES; CATALYSIS; COENZYMES; CONSERVED SEQUENCE; COPPER; DIHYDROXYPHENYLALANINE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ETHYLAMINES; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHENYLHYDRAZINES; PICHIA; TYROSINE;

PICHIA ANGUSTA;

EID: 33644863935     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052025m     Document Type: Article

References (37)

1. Janes, S. M., Mu, D., Wemmer, D., Smith, A. J., Kaur, S., Maltby, D., Burlingame, A. L., and Klinman, J. P. (1990) A new redox cofactor in eukaryotic enzymes: Identification of 6-hydroxydopa at the active site of bovine serum amine oxidase, Science 248, 981-987.
2. Mu, D., Janes, S. M., Smith, A. J., Brown, D. E., Dooley, D. M., and Klinman, J. P. (1992) Codon identification for 6-hydroxydopa at the active site of the amine oxidase from the yeast Hansenula polymorpha, J. Biol. Chem. 267, 7979-7982.
3. Cai, D. Y., and Klinman, J. P. (1994) Evidence for a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase, J. Biol. Chem. 269, 32039-32042.
4. McIntire, W. S., Wemmer, D. E., Christoserdov, A. Y., and Lidstrom, M. E. (1991) A new cofactor in a prokaryotic enzyme: Tyrptophan tryptophylquinone as the redox prosthetic group of methylamine dehydrogenase, Science 252, 817-824.
5. Datta, S., Mori, Y., Takagi, K., Kawaguchi, K., Chen, Z.-W., Okajima, T., Kuroda, S., Ikeda, T., Kano, K., Tanizawa, K., and Mathews, F. S. (2001) Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking, Proc. Natl. Acad. Sci. U.S.A. 98, 14268-14273.
6. Wang, S., Mure, M., Medsihradszky, K. F., Burlingame, A. L., Brown, D. E., Dooley, D. M., Smith, A. J., Kagan, A. M., and Klinman, J. P. (1996) A crosslinked cofactor in lysyl oxidase: Redox function for amino acid side chains, Science 273, 1078-1084.
7. Dove, J. E., Schwartz, B., Williams, N. K., and Klinman, J. P. (2000) Investigation of spectroscopic intermediates during copper-binding and TPQ formation in wild-type and active-site mutants of a copper-containing amine oxidase from yeast, Biochemistry 39, 3690-3698.
8. Schwartz, B., Dove, J. E., and Klinman, J. P. (2000) Kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast, Biochemistry 39, 3699-3707.
9. Schwartz, B., Olgin, A., and Klinman, J. P. (2001) The role of copper in topa quinone biogenesis and catalysis, as probed by azide inhibition of a copper amine oxidase from yeast, Biochemistry 40, 2954-2963.
10. Ruggiero, C. E., and Dooley, D. M. (1999) Stoichiometry of the topa quinone biogenesis reaction in copper amine oxidases, Biochemistry 38, 2892-2898.
11. Kim, M., Okajima, T., Kishishita, S., Yoshimura, M., Kawamori, A., Tanizawa, K., and Yamaguchi, H. (2002) X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase, Nat. Struct. Biol. 9, 591-596.
12. Mure, M., Mills, S. A., and Klinman, J. P. (2002) Catalytic mechanism of the topa quinone containing copper amine oxidase, Biochemistry 41, 9269-9278.
13. Green, E. L., Nakamura, N., Dooley, D. M., Klinman, J. P., and Sanders-Loehr, J. (2002) Rates of oxygen and hydrogen exchange as indicators of TPQ cofactor orientation in amine oxidase, Biochemistry 41, 687-696.
14. Kumar, V., Dooley, D. M., Freeman, H. C., Guss, J. M., Harvey, I., McGuirl, M. A., Wilce, M. C. J., and Zubak, V. M. (1996) Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 Å resolution, Structure 4, 943-955.
15. Li, R. B., Klinman, J. P., and Mathews, F. S. (1998) Crystal structure of copper amine oxidase from Hansenula polymorpha determined at 2.4 Å resolution, Structure 6, 293-307.
16. Murray, J. M., Kurtis, C. R., Tambyrajah, W., Saysell, C. G., Wilmot, C. M., Parsons, M. R., Phillips, S. E. V., Knowles, P. F., and McPherson, M. J. (2001) Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential, Biochemistry 40, 12808-12818.
17. Chen, Z. W., Schwartz, B., Williams, N. K., Li, R. B., Klinman, J. P., and Mathews, F. S. (2000) Crystal structure at 2.5 Å resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli, Biochemistry 39, 9709-9717.
18. Hevel, J. M., Mills, S. A., and Klinman, J. P. (1999) Mutation of a strictly conserved active site residue alters substrate specificity and cofactor biogenesis in a copper amine oxidase, Biochemistry 38, 3683-3693.
19. Cai, D. Y., and Klinman, J. P. (1994) Copper amine oxidase: Heterologous expression, purification and characterization of an active enzyme in Saccharomyces cerevisiae, Biochemistry 33, 7647-7653.
20. Palcic, M., and Janes, S. M. (1995) Spectrophotometric detection of topa quinone, in Redox-Active Amino Acids in Biology (Klinman, J. P., Ed.) pp 34-38, Academic Press, San Diego.
21. Gay, C., Collins, J., and Gebicki, J. M. (1999) Hydroperoxide assay with the ferric-xylenol orange complex, Anal. Biochem. 273, 149-155.
22. Gay, C. A., and Gebicki, J. M. (2002) Perchloric acid enhances sensitivity and reproducibility of the ferric-xylenol orange peroxide assay. Anal. Biochem. 304, 42-46.
23. Gay, C. A., and Gebicki, J. A. (2003) Measurement of protein and lipid hydroperoxides in biological systems by the ferric-xylenol orange method, Anal. Biochem. 315, 29-35.
24. Samuels, N., and Klinman, J. P. (2005) 2,4,5-Trihydroxyphenylalanine Quinone Biogenesis in the Copper Amine Oxidase from Hansenula polymorpha with the Alternate Metal, Nickel, Biochemistry 44, 14308-14317.
25. Parsons, M. R., Convery, M. A., Wilmot, C. M., Yadav, K. D. S., Blakely, V., Corner, A. S., Philips, S. E. V., McPherson, M. J., and Knowles, P. F. (1995) Crystal structure of a quinoenzyme: Copper amine oxidase of Escherichia coli at 2 Å resolution, Structures, 1171-1184.
26. Wilce, M. C. J., Dooley, D. M., Freeman, H. C., Guss, J. M., Matsunami, H., McIntire, W. S., Ruggiero, C. E., Tanizawa, K., and Yamaguchi, H. (1997) Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: Implications for the biogenesis of topaquinone, Biochemistry 36, 16116-16133.
27. Murray, J. M., Saysell, C. G., Wilmot, C. M., Tambyrajah, W. S., Jaeger, J., Knowles, P. F., Philips, S. E. V., and McPherson, M. J. (1999) Amine oxidase: X-ray crystallographic studies with mutational variants, Biochemistry 38, 8217-8227.
28. Airenne, T. T., Nymalm, Y., Kidron, H., Smith, D. J., Pihlavisto, M., Salmi, M., Jalkanen, S., Johnson, M. S., and Salminen, T. A. (2005) Crystal structure of the human vascular adhesion protein-1. Unique structural features with functional implications. Protein Sci. 14, 1964-1974.
29. Duff, A. P., Cohen, A. E., Ellis, P. J., Kuchar, J. A., Langley, D. B., Shepard, E. M., Dooley, D. M., Freeman, H. C., and Guss, J. M. (2003) The crystal structure of Pichia pastoris lysyl oxidase, Biochemistry 42, 15148-15157.
30. Plastino, J., Green, E. L., Sanders-Loehr, J., and Klinman, J. P. (1999) An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha, Biochemistry 38, 8204-8216.
31. Mure, M., and Klinman, J. P. (1995) Model studies of topaquinone- dependent amine oxidases. II. characterization of reaction intermediates and mechanism, J. Am. Chem. Soc. 117, 8707-8718.
32. Mure, M., and Klinman, J. P. (1993) Synthesis and spectroscopic characterization of model compounds for the active site cofactor in copper amine oxidase, J. Am. Chem. Soc. 115, 7117-7127.
33. M-OOH intermediate, Biochemistry 43, 5735-5747.
34. Cai, D. Y., Dove, J., Nakamura, N., Sanders-Loehr, J., and Klinman, J. P. (1997) Mechanism-based inactivation of a yeast methylamine oxidase mutant: Implications for the functional role of the consensus sequence surrounding topa quinone, Biochemistry 36, 11472-11478.
35. Schwartz, B., Green, E. L., Sanders-Loehr, J., and Klinman, J. P. (1998) The relation between conserved consensus site residues and the productive conformation for TPQ cofactor in a copper-containing amino oxidase from yeast, Biochemistry 37, 16591-16600.
36. Nakamura, N., Moenne-Loccoz, P., Tanizawa, K., Mure, M., Suzuki, S., Klinman, J. P., and Sanders-Loehr, J. (1997) Topaquinone-dependent amine oxidases: Identification of reaction intermediates by Raman spectroscopy, Biochemistry 36, 11479-11486.
37. Wilmot, C. H., Murray, J. M., Alton, G., Parsons, M. R., Convery, M. A., Blakeley, V., Corner, A. S., Palcic, M. M., Knowles, P. R, McPherson, M. J., and Phillips, S. E. (1997) Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: Exploring the reductive half reaction, Biochemistry 36, 1608-1620.