Aspergillus fumigatus SidA Is a highly specific ornithine hydroxylase with bound flavin cofactor

Biochemistry

Volumn 49, Issue 31, 2010, Pages 6777-6783

  Chocklett, Samuel W ^a   Sobrado, Pablo ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPERGILLUS FUMIGATUS; CATALYTIC EFFICIENCIES; FLAVIN COFACTOR; HIGH CONCENTRATION; HYDROXAMATE; HYDROXYLASES; IRON BINDING; KINETIC MECHANISM; LIMITING CONDITION; MONOOXYGENASES; PATHOGENIC FUNGI; SATURATION KINETICS; SIDEROPHORES; SUBSTRATE INHIBITION; TERNARY COMPLEX; TETRAMERS;

AMIDES; AMINO ACIDS; BIOCHEMISTRY; HYDROGEN PEROXIDE; HYDROXYLATION; ORGANIC ACIDS; REACTION INTERMEDIATES;

ENZYME INHIBITION;

AMINO ACID; FERRICHROME; HYDROGEN PEROXIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; ORNITHINE; ORNITHINE HYDROXYLASE; OXYGENASE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SIDEROPHORE; SIDEROPHORE A; UNCLASSIFIED DRUG;

ARTICLE; ASPERGILLUS FUMIGATUS; BINDING AFFINITY; CATALYSIS; CHEMICAL REACTION KINETICS; COMPLEX FORMATION; CONCENTRATION RESPONSE; HYDROXYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ASPERGILLUS FUMIGATUS; CATALYSIS; FLAVINS; KINETICS; MIXED FUNCTION OXYGENASES; NADP; ORNITHINE; SIDEROPHORES;

ASPERGILLUS FUMIGATUS; FUNGI;

EID: 77955251194     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100291n     Document Type: Article

References (26)

1. Marr, K. A., Patterson, T., and Denning, D. (2002) Aspergillosis. Pathogenesis, clinical manifestations, and therapy Infect. Dis. Clin. North. Am. 16, 875-894, vi
2. Denning, D. W. (2002) Echinocandins: a new class of antifungal J. Antimicrob. Chemother. 49, 889-891
3. Tekaia, F. and Latge, J. P. (2005) Aspergillus fumigatus: saprophyte or pathogen? Curr. Opin. Microbiol. 8, 385-392
4. Frederick, R. E., Mayfield, J. A., and DuBois, J. L. (2009) Iron trafficking as an antimicrobial target Biometals 22, 583-593
5. Fischbach, M. A., Lin, H., Liu, D. R., and Walsh, C. T. (2006) How pathogenic bacteria evade mammalian sabotage in the battle for iron Nat. Chem. Biol. 2, 132-138
6. Rementeria, A., Lopez-Molina, N., Ludwig, A., Vivanco, A. B., Bikandi, J., Ponton, J., and Garaizar, J. (2005) Genes and molecules involved in Aspergillus fumigatus virulence Rev. Iberoam. Micol. 22, 1-23
7. Haas, H. (2006) Fungal siderophores: their role in disease Annu. Rev. Phytopathol. 46, 149-187
8. 5-oxygenase, is required for virulence Infect. Immun. 73, 5493-5503
9. Schrettl, M., Bignell, E., Kragl, C., Sabiha, Y., Loss, O., Eisendle, M., Wallner, A., Arst, H. N., Jr., Haynes, K., and Haas, H. (2007) Distinct roles for intra- and extracellular siderophores during Aspergillus fumigatus infection PLoS Pathog. 3, 1195-1207
10. Visca, P., Serino, L., and Orsi, N. (1992) Isolation and characterization of Pseudomonas aeruginosa mutants blocked in the synthesis of pyoverdin J. Bacteriol. 174, 5727-5731
11. Sokol, P. A., Darling, P., Woods, D. E., Mahenthiralingam, E., and Kooi, C. (1999) Role of ornibactin biosynthesis in the virulence of Burkholderia cepacia: characterization of pvdA, the gene encoding l -ornithine N(5)-oxygenase Infect. Immun. 67, 4443-4455
12. Takase, H., Nitanai, H., Hoshino, K., and Otani, T. (2000) Impact of siderophore production on Pseudomonas aeruginosa infections in immunosuppressed mice Infect. Immun. 68, 1834-1839
13. Blommel, P. G., Martin, P. A., Seder, K. D., Wrobel, R. L., and Fox, B. G. (2009) Flexi vector cloning Methods Mol. Biol. 498, 55-73
14. Csaky, T. (1948) On the estimation of bound hydroxylamine in biological materials Acta Chem. Scand. 450-454
15. Hildebrandt, A. G., Roots, I., Tjoe, M., and Heinemeyer, G. (1978) Hydrogen peroxide in hepatic microsomes Methods Enzymol. 52, 342-350
16. Meneely, K. M. and Lamb, A. L. (2007) Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism Biochemistry 46, 11930-11937
17. Massey, V. (2000) The chemical and biological versatility of riboflavin Biochem. Soc. Trans. 28, 283-296
18. van Berkel, W. J., Kamerbeek, N. M., and Fraaije, M. W. (2006) Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts J. Biotechnol. 124, 670-689
19. Quadri, L. E., Sello, J., Keating, T. A., Weinreb, P. H., and Walsh, C. T. (1998) Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin Chem. Biol. 5, 631-645
20. 6-hydroxylase. Effect of a mutation in the assumed FAD binding site on coenzyme affinities and on lysine hydroxylating activity Biol. Chem. 380, 47-54
21. 6-hydroxylase Biochim. Biophys. Acta 1343, 263-277
22. 6-hydroxylase: stability and interaction with ligands J. Protein Chem. 18, 893-903
23. Ziegler, D. M. (2002) An overview of the mechanism, substrate specificities, and structure of FMOs Drug Metab. Rev. 34, 503-511
24. Torres Pazmino, D. E., Baas, B. J., Janssen, D. B., and Fraaije, M. W. (2008) Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca Biochemistry 47, 4082-4093
25. Alfieri, A., Malito, E., Orru, R., Fraaije, M. W., and Mattevi, A. (2008) Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase Proc. Natl. Acad. Sci. U.S.A. 105, 6572-6577
26. 2 addition but not flavin reduction Biochemistry 48, 4371-4376