Tyrosine-Derived Quinone Cofactors

Accounts of Chemical Research

Volumn 37, Issue 2, 2004, Pages 131-139

  Mure, Minae ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2,4,5 TRIHYDROXYPHENYLALANINE QUINONE; 2,4,5-TRIHYDROXYPHENYLALANINE QUINONE; AMINE OXIDASE (COPPER CONTAINING); COBALT; COPPER AMINE OXIDASE; COPPER DERIVATIVE; DOPA; DRUG DERIVATIVE; LYSINE; LYSINE TYROSYLQUINONE; NICKEL; OXIDOREDUCTASE; PROTEIN LYSINE 6 OXIDASE; QUINONE DERIVATIVE; TYROSINE; UNCLASSIFIED DRUG;

ANIMAL; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COENZYME; ENZYME ACTIVE SITE; HUMAN; METABOLISM; OXIDATION; REACTION ANALYSIS; STRUCTURE ANALYSIS; SYNTHESIS;

AMINE OXIDASE (COPPER-CONTAINING); ANIMALS; BINDING SITES; COENZYMES; DIHYDROXYPHENYLALANINE; HUMANS; LYSINE; MODELS, MOLECULAR; PROTEIN-LYSINE 6-OXIDASE; QUINONES;

EID: 1242338900     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar9703342     Document Type: Article

References (49)

1. Principles and Applications of Quinoproteins; Davidson, V. L., Ed.; Dekker: New York, 1993.
2. Janes, S. M.; Mu, D.; Wemmer, D.; Smith, A. J.; Kaur, S.; Maltby, D.; Burlingame, A. L.; Klinman, J. P. A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine Oxidase. Science 1990, 248, 981-987.
3. Wang, S. X.; Mure, M.; Medzihradszky, K. F.; Burlingame, A. L.; Brown, D. E.; Dooley, D. M.; Smith, A. J.; Kagan, H. M.; Klinman, J. P. A Cross-linked Cofactor in Lysyl Oxidase-Redox Function for Amino Acid Side Chains. Science 1996, 273, 1078-1084.
4. McIntire, W. S.; Wemmer, D. E.; Chistoserdov, A.; Lidstrom, M. E. A New Cofactor in a Prokaryotic Enzyme - Tryptophan Tryptophylquinone as the Redox Prosthetic Group in Methylamine Dehydrogenase. Science 1991, 252, 817-824.
5. Satoh, A.; Kim, J. K.; Miyahara, I.; Devreese, B.; Vandenberghe, I.; Hacisalihoglu, A.; Okajima, T.; Kuroda, S.; Adachi, O.; Duine, J. A.; Van Beeumen, J.; Tanizawa, K.; Hirotsu, K. Crystal Structure of Quinohemoprotein Amine Dehydrogenase from Pseudomonas putida - Identification of a Novel Quinone Cofactor Encaged by Multiple Thioether Cross-bridges. J. Biol. Chem. 2002, 277, 2830-2834.
6. Kasahara, T.; Kato, T. A New Redox-Cofactor Vitamin for Mammals. Nature 2003, 422, 832.
7. Klinman, J. P. New Quinocofactors in Eukaryotes. J. Biol. Chem. 1996, 271, 27189-27192.
8. Kim, M.; Okajima, T.; Kishishita, S.; Yoshimura, M.; Kawamori, A.; Tanizawa, K.; Yamaguchi, H. X-ray Snapshots of Quinone Cofactor Biogenesis in Bacterial Copper Amine Oxidase. Nat. Struct. Biol. 2002, 9, 591-596.
9. Klinman, J. P.; Mu, D. Quinoenzymes in Biology. Annu. Rev. Biochem. 1994, 63, 299-344.
10. Mure, M.; Mills, S. A.; Klinman, J. P. Catalytic Mechanism of the Topa Quinone Containing Copper Amine Oxidases. Biochemistry 2002, 41, 9269-9278.
11. Csiszar, K. Lysyl Oxidases: A Novel Multifunctional Amine Oxidase Family. Prog. Nucleic Acid Res. Mol. Biol. 2001, 70, 1-32.
12. Jalkanen, S.; Salmi, M. Cell Surface Monoamine Oxidases: Enzymes in Search of a Function. EMBO J. 2001, 20, 3893-3901.
13. Mure, M.; Klinman, J. P. Synthesis and Spectroscopic Characterization of Model Compounds for the Active Site Cofactor in Copper Amine Oxidases. J. Am. Chem. Soc. 1993, 115, 7117-7127.
14. Mure, M.; Klinman, J. P. Model Studies of Topaquinone-Dependent Amine Oxidases. 1. Oxidation of Benzylamine by Topaquinone Analogues. J. Am. Chem. Soc. 1995, 117, 8698-8706.
15. Li, R.; Klinman, J. P.; Mathews, F. S. Copper Amine Oxidase from Hansenula polymorpha: The Crystal Structure Determined at 2.4 A Resolution Reveals the Active Conformation. Structure 1998, 6, 293-307.
16. Kishishita, S.; Okajima, T.; Kim, M.; Yamaguchi, H.; Hirota, S.; Suzuki, S.; Kuroda, S.; Tanizawa, K.; Mure, M. Role of Copper Ion in Bacterial Copper Amine Oxidase: Spectroscopic and Crystallographic Studies of Metal-substituted Enzymes. J. Am. Chem. Soc. 2003, 125, 1041-1055.
17. Murray, J. M.; Saysell, C. G.; Wilmot, C. M.; Tambyrajah, W. S.; Jaeger, J.; Knowles, P. F.; Phillips, S. E.; McPherson, M. J. The Active Site Base Controls Cofactor Reactivity in Escherichia coli Amine Oxidase: X-ray Crystallographic Studies with Mutational Variants. Biochemistry 1999, 38, 8217-8227.
18. Parsons, M. R.; Convery, M. A.; Wilmot, C. M.; Yadav, K. D.; Blakeley, V.; Corner, A. S.; Phillips, S. E.; McPherson, M. J.; Knowles, P. F. Crystal Structure of a Quinoenzyme: Copper Amine Oxidase of Escherichia coli at 2 A Resolution. Structure 1995, 3, 1171-1184.
19. Wilce, M. C.; Dooley, D. M.; Freeman, H. C.; Guss, J. M.; Matsunami, H.; McIntire, W. S.; Ruggiero, C. E.; Tanizawa, K.; Yamaguchi, H. Crystal Structures of the Copper-containing Amine Oxidase from Arthrobacter globiformis in the Holo and Apo Forms: Implications for the Biogenesis of Topaquinone. Biochemistry 1997, 36, 16116-16133.
20. Kumar, V.; Dooley, D. M.; Freeman, H. C.; Guss, J. M.; Harvey, I.; McGuirl, M. A.; Wilce, M. C.; Zubak, V. M. Crystal Structure of a Eukaryotic (Pea Seedling) Copper-containing Amine Oxidase at 2.2 A Resolution. Structure 1996, 4, 943-955.
21. Murray, J. M.; Kurtis, C. R.; Tambyrajah, W.; Saysell, C. G.; Wilmot, C. M.; Parsons, M. R.; Phillips, S. E. V.; Knowles, P. F.; McPherson, M. J. Conserved Tyrosine-369 in the Active Site of Escherichia coli Copper Amine Oxidase Is Not Essential. Biochemistry 2001, 40, 12808-12818.
22. Plastino, J.; Green, E. L.; Sanders-Loehr, J.; Klinman, J. P. An Unexpected Role for the Active Site Base in Cofactor Orientation and Flexibility in the Copper Amine Oxidase from Hansenula polymorpha. Biochemistry 1999, 38, 8204-8216.
23. Mure, M.; Brown, D. E.; Kurtis, C. R.; Saysell, C. G.; Rogers, M.; Parsons, M. R.; Wilmot, C. M.; Phillips, S. E. V.; McPherson, M. J.; Knowles, P. F.; Dooley, D. M. Manuscript in preparation.
24. Cai, D. Y.; Dove, J.; Nakamura, N.; SandersLoehr, J.; Klinman, J. P. Mechanism-based Inactivation of a Yeast Methylamine Oxidase Mutant: Implications for the Functional Role of the Consensus Sequence Surrounding Topaquinone. Biochemistry 1997, 36, 11472-11478.
25. Schwartz, B.; Green, E. L.; Sanders-Loehr, J.; Klinman, J. P. Relationship between Conserved Consensus Site Residues and the Productive Conformation for the TPQ Cofactor in a Copper-containing Amine Oxidase from Yeast. Biochemistry 1998, 37, 16591-16600.
26. Hevel, J. M.; Mills, S. A.; Klinman, J. P. Mutation of a Strictly Conserved, Active-Site Residue Alters Substrate Specificity and Cofactor Biogenesis in a Copper Amine Oxidase. Biochemistry 1999, 38, 3683-3693.
27. Wilmot, C. M.; Murray, J. M.; Alton, G.; Parsons, M. R.; Convery, M. A.; Blakeley, V.; Corner, A. S.; Palcic, M. M.; Knowles, P. F.; McPherson, M. J.; Phillips, S. E. Catalytic Mechanism of the Quinoenzyme Amine Oxidase from Escherichia coli: Exploring the Reductive Half-reaction. Biochemistry 1997, 36, 1608-1620.
28. Farnum, M.; Palcic, M.; Klinman, J. P. pH Dependence of Deuterium Isotope Effects and Tritium Exchange in the Bovine Plasma Amine Oxidase Reaction: A Role for Single-base Catalysis in Amine Oxidation and Imine Exchange. Biochemistry 1986, 25, 1898-1904.
29. Su, Q. J.; Klinman, J. P. Probing the Mechanism of Proton Coupled Electron Transfer to Dioxygen: The Oxidative Half-reaction of Bovine Serum Amine Oxidase. Biochemistry 1998, 37, 12513-12525.
30. Mills, S. A.; Goto, Y.; Su, Q.; Plastino, J. J.; Klinman, J. P. Co-HPAO Has the Same Mechanism as WT-HPAO. Biochemistry 2002, 41, 10577-10584.
31. Goto, Y.; Klinman, J. P. Binding of Dioxygen to Non-Metal Sites in Proteins: Exploration of the Importance of Binding Site Size versus Hydrophobicity in the Copper Amine Oxidase from Hansenula polymorpha. Biochemistry 2001, 41, 13637-13643.
32. Dooley, D. M.; McGuirl, M. A.; Brown, D. E.; Turowski, P. N.; McIntire, W. S.; Knowles, P. F. A Cu(I)-semiquinone State in Substrate-reduced Amine Oxidases. Nature 1991, 349, 262-264.
33. Wilmot, C. M.; Hajdu, J.; McPherson, M. J.; Knowles, P. F.; Phillips, S. E. Visualization of Dioxygen Bound to Copper During Enzyme Catalysis. Science 1999, 286, 1724-1728.
34. Hirota, S.; Iwamoto, T.; Kishishita, S.; Okajima, T.; Yamauchi, O.; Tanizawa, K. Spectroscopic Observation of Intermediates Formed durng the Oxidative Half-Reaction of Copper/Topa Quinone-Containing PhenyJethylamine Oxidase. Biochemistry 2001, 40, 15789-15796.
35. 1H Nuclei. J. Am. Chem. Soc. 1994, 116, 4028-4037.
36. Bisby, R. H.; Johnson, S. A.; Parker, A. W. Radicals from One-Electron Oxidation of 4-Aminoresorcinol: Models for the Active Site Radical Intermediate in Copper Amine Oxidases. J. Phys. Chem. B 2000, 104, 5832-3829.
37. + During Dioxygen Activation in a Copper Amine Oxidase from Yeast. J. Am. Chem. Soc. 2000, 122, 9897-9904.
38. Zhang, L.; Bandy, B.; Davison, A. J. Effect of Metals, Ligands and Antioxidants on the Reaction of Oxygen with 1,2,4-Benzenetriol. Free Radical Biol. Med. 1996, 20, 495-505.
39. Mure, M.; Klinman, J. P. Model Studies of Topaquinone-Dependent Amine Oxidases. 2. Characterization of Reaction Intermediates and Mechanism. J. Am. Chem. Soc. 1995, 117, 8707-8718.
40. SmithMungo, L. I.; Kagan, H. M. Lysyl oxidase: Properties, Regulation and Multiple Functions in Biology. Matrix Biol. 1998, 16, 387-398.
41. Kirschmann, D. A.; Seftor, E. A.; Fong, S. F. T.; Nieva, D. R. C.; Sullivan, C. M.; Edwards, E. M.; Sommer, P.; Csiszar, K.; Hendrix, M. J. C. A Molecular Role for Lysyl Oxidase in Breast Cancer Invasion. Cancer Res. 2002, 62, 4478-4483.
42. Kenyon, K.; Contente, S.; Trackman, P. C.; Tang, J.; Kagan, H. M.; Friedman, R. M. Lysyl Oxidase and rrg Messenger RNA. Science 1991, 253, 802-802.
43. Gacheru, S. N.; Trackman, P. C.; Kagan, H. M. Evidence for a Functional Role for Histidine in Lysyl Oxidase Catalysis. J. Biol. Chem. 1988, 263, 16704-16708.
44. Gacheru, S. N.; Trackman, P. C.; Shah, M. A.; Ogara, C. Y.; Spacciapoli, P.; Greenaway, F. T.; Kagan, H. M. Structural and Catalytic Properties of Copper in Lysyl Oxidase. J. Biol. Chem. 1990, 265, 19022-19027.
45. Tang, C.; Klinman, J. P. The Catalytic Function of Bovine Lysyl Oxidase in the Absence of Copper. J. Biol. Chem. 2001, 276 (33), 30575-30578.
46. Mure, M.; Wang, S. X.; Klinman, J. P. Synthesis and Characterization of Model Compounds of the Lysyl Tyrosine Quinone (LTQ) Cofactor of Lysyl Oxidase. J. Am. Chem. Soc. 2003, 125, 6113-6125.
47. Wang, S. X.; Nakamura, N.; Mure, M.; Klinman, J. P.; Sanders-Loehr, J. Characterization of the Native Lysine Tyrosylquinone Cofactor in Lysyl Oxidase by Raman Spectroscopy. J. Biol. Chem. 1997, 272, 28841-28844.
48. Hess, C. R.; Juda, G. A.; Dooley, D. M.; Amii, R. N.; Hill, M. G.; Winkler, J. R.; Gray, H. B. Gold Electrodes Wired for Coupling with the Deeply Buried Active Site of Arthrobacter globiformis Amine Oxidase. J. Am. Chem. Soc. 2003, 125 (24), 7156-7157.
49. Janes, S. M.; Palcic, M. M.; Scaman, C. H.; Smith, A. J.; Brown, D. E.; Dooley, D. M.; Mure, M.; Klinman, J. P. Identification of Topaquinone and Its Consensus Sequence in Copper Amine Oxidases. Biochemistry 1992, 31, 12147-12154.