Functional role of Trp-105 of Enterococcus faecalis azoreductase (AzoA) as resolved by structural and mutational analysis

Microbiology

Volumn 154, Issue 9, 2008, Pages 2659-2667

  Chen, Huizhong ^a   Xu, Haiyan ^a   Kweon, Ohgew ^a   Chen, Siwei ^a   Cerniglia, Carl E ^a  

^a NATIONAL CENTER FOR TOXICOLOGICAL RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ASPARAGINE; AZO REDUCTASE; FLAVINE MONONUCLEOTIDE; GLUTAMINE; GLYCINE; HISTIDINE; LEUCINE; PHENYLALANINE; TRYPSIN; TYROSINE; OXIDOREDUCTASE; TRYPTOPHAN;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; BINDING AFFINITY; CATALYSIS; COMPUTER ANALYSIS; CONTROLLED STUDY; ENTEROCOCCUS FAECALIS; ENZYME ACTIVITY; ENZYME BINDING; ENZYME STRUCTURE; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; GENE OVEREXPRESSION; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; SEQUENCE ALIGNMENT; STRUCTURE ACTIVITY RELATION;

ENTEROCOCCUS FAECALIS; ESCHERICHIA COLI;

AMINO ACID SEQUENCE; BINDING SITES; CLONING, MOLECULAR; ENTEROCOCCUS FAECALIS; ESCHERICHIA COLI; FLAVIN MONONUCLEOTIDE; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; NADH, NADPH OXIDOREDUCTASES; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TRYPTOPHAN;

EID: 53449100677     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.2008/019877-0     Document Type: Article

References (25)

1. Chen, H. (2006). Recent advances in azo dye degrading enzyme research. Curr Protein Pept Sci 7, 101-111.
2. Chen, H., Wang, R. F. & Cerniglia, C. E. (2004). Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis. Protein Expr Purif 34, 302-310.
3. Chen, H., Hopper, S. L. & Cerniglia, C. E. (2005). Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein. Microbiology 151, 1433-1441.
4. Chung, K. T. (1983). The significance of azo-reduction in the mutagenesis and carcinogenesis of azo dyes. Mutat Res 114, 269-281.
5. Deller, S., Sollner, S., Trenker-El-Toukhy, R., Jelesarov, I., Gubitz, G. M. & Macheroux, P. (2006). Characterization of a thermostable NADPH:FMN oxidoreductase from the mesophilic bacterium Bacillus subtilis. Biochemistry 45, 7083-7091.
6. Eckburg, P. B., Bik, E. M., Bernstein, C. N., Purdom, E., Dethlefsen, L., Sargent, M., Gill, S. R., Nelson, K. E. & Relman, D. A. (2005). Diversity of the human intestinal microbial flora. Science 308, 1635-1638.
7. Hanauer, S. B. (1996). Inflammatory bowel disease. N Engl J Med 334, 841-848.
8. Ito, K., Nakanishi, M., Lee, W. C., Sasaki, H., Zenno, S., Saigo, K., Kitade, Y. & Tanokura, M. (2006). Three-dimensional structure of AzoR from Escherichia coli. An oxidoreductase conserved in micro-organisms. J Biol Chem 281, 20567-20576.
9. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
10. Li, Z. & Meighen, E. A. (1995). Tryptophan 250 on the alpha subunit plays an important role in flavin and aldehyde binding to bacterial luciferase. Effects of W→Y mutations on catalytic function. Biochemistry 34, 15084-15090.
11. Liu, Z. J., Chen, H., Shaw, N., Hopper, S. L., Chen, L., Chen, S., Cerniglia, C. E. & Wang, B. C. (2007). Crystal structure of an aerobic FMN-dependent azoreductase (AzoA) from Enterococcus faecalis. Arch Biochem Biophys 463, 68-77.
12. Lostao, A., Gomez-Moreno, C., Mayhew, S. G. & Sancho, J. (1997). Differential stabilization of the three FMN redox forms by tyrosine 94 and tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials. Biochemistry 36, 14334-14344.
13. Lostao, A., Daoudi, F., Irun, M. P., Ramon, A., Fernandez-Cabrera, C., Romero, A. & Sancho, J. (2003). How FMN binds to Anabaena apoflavodoxin: A hydrophobic encounter at an open binding site. J Biol Chem 278, 24053-24061.
14. Maiti, R., Van Domselaar, G. H., Zhang, H. & Wishart, D. S. (2004). SuperPose: A simple server for sophisticated structural superposition. Nucleic Acids Res 32, W590-W594.
15. McDonald, I. K. & Thornton, J. M. (1994). Satisfying hydrogen bonding potential in proteins. J Mol Biol 238, 777-793.
16. Milburn, D., Laskowski, R. A. & Thornton, J. M. (1998). Sequences annotated by structure: A tool to facilitate the use of structural information in sequence analysis. Protein Eng 11, 855-859.
17. Murray, T. A. & Swenson, R. P. (2003). Mechanism of flavin mononucleotide cofactor binding to the Desulfovibrio vulgaris flavodoxin. 1. Kinetic evidence for cooperative effects associated with the binding of inorganic phosphate and the 5′-phosphate moiety of the cofactor. Biochemistry 42, 2307-2316.
18. Platzek, T., Lang, C., Grohmann, G., Gi, U. S. & Baltes, W. (1999). Formation of a carcinogenic aromatic amine from an azo dye by human skin bacteria in vitro. Hum Exp Toxicol 18, 552-559.
19. Schwede, T., Kopp, J., Guex, N. & Peitsch, M. C. (2003). SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res 31, 3381-3385.
20. Sobolev, V., Sorokine, A., Prilusky, J., Abola, E. E. & Edelman, M. (1999). Automated analysis of interatomic contacts in proteins. Bioinformatics 15, 327-332.
21. Stolz, A. (2001). Basic and applied aspects in the microbial degradation of azo dyes. Appl Microbiol Biotechnol 56, 69-80.
22. Velec, H. F., Gohlke, H. & Klebe, G. (2005). DrugScore (CSD)-knowledge-based scoring function derived from small molecule crystal data with superior recognition rate of near-native ligand poses and better affinity prediction. J Med Chem 48, 6296-6303.
23. Wallace, A. C., Laskowski, R. A. & Thornton, J. M. (1995). LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8, 127-134.
24. Wang, C. J., Hagemeier, C., Rahman, N., Lowe, E., Noble, M., Coughtrie, M., Sim, E. & Westwood, I. (2007). Molecular cloning, characterisation and ligand-bound structure of an azoreductase from Pseudomonas aeruginosa. J Mol Biol 373, 1213-1228.
25. Wu, K., Knox, R., Sun, X. Z., Joseph, P., Jaiswal, A. K., Zhang, D., Deng, P. S. & Chen, S. (1997). Catalytic properties of NAD(P)H: quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase. Arch Biochem Biophys 347, 221-228.