Site-directed mutagenesis of substrate binding sites of azoreductase from Rhodobacter sphaeroides

Biotechnology Letters

Volumn 30, Issue 5, 2008, Pages 869-875

  Liu, Guangfei ^a   Zhou, Jiti ^a   Wang, Jing ^a   Yan, Bin ^b   Li, Jingmei ^a   Lu, Hong ^a   Qu, Yuanyuan ^a   Jin, Ruofei ^a  

^a DALIAN UNIVERSITY OF TECHNOLOGY   (China)

^b XIAMEN UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

Azoreductase; Flavodoxin; Nitroreductase; Rhodobacter sphaeroides; Site directed mutagenesis

Indexed keywords

BINDING SITES; NUCLEOTIDES; PH EFFECTS; SUBSTRATES;

AZOREDUCTASE; FLAVIN MONONUCLEOTIDE (FMN); FLAVODOXIN; POSITIVELY CHARGED RESIDUES; RHODOBACTER SPHAEROIDES;

MUTAGENESIS;

AZO COMPOUND; AZO REDUCTASE; METHYL RED; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMISTRY; CHROMOTROPE FB; COMPARATIVE STUDY; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR GENETICS; PH; PLASMID; PROTEIN TERTIARY STRUCTURE; RHODOBACTER SPHAEROIDES; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; TEMPERATURE;

AMINO ACID SEQUENCE; AZO COMPOUNDS; BINDING SITES; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NADH, NADPH OXIDOREDUCTASES; NADP; PLASMIDS; PROTEIN STRUCTURE, TERTIARY; RHODOBACTER SPHAEROIDES; SEQUENCE ALIGNMENT; TEMPERATURE;

RHODOBACTER SPHAEROIDES;

EID: 41549168117     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-007-9627-8     Document Type: Article

References (25)

1. Bellamacina CR (1996) The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins. FASEB J 10:1257-1269
2. Bottoms CA, Smith PE, Tanner JJ (2002) A structurally conserved water molecule in Rossmann fold dinucleotide-binding domains. Protein Sci 11:2125-2137
3. Chen H (2006) Recent advances in azo dye degrading enzyme research. Curr Protein Pept Sci 7:101-111
4. Chen H, Hopper SL, Cerniglia CE (2005) Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein. Microbiology 151:1433-1441
5. Chung KT (1983) The significance of azo-reducion in the mutagenesis and carcinogenesis of azo dyes. Mutat Res 114:269-281
6. DeLano WL (2003) PyMOL reference manual. DeLano Scientific LLC, San Carlos
7. Dos Santos AB, Cervantes FJ, Van Lier JB (2007) Review paper on current technologies for decolourisation of textile wastewaters: perspectives for anaerobic biotechnology. Biores Technol 98:2369-2385
8. Freigang J, Diederichs K, Schäfer KP, Welte W, Paul R (2002) Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori. Protein Sci 11:253-261
9. Hanauer SB (1996) Inflammatory bowel disease. N Engl J Med 334:841-848
10. Ito K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M (2006) Three-dimensional structure of AzoR from Escherichia coli. An oxidereductase conserved in microorganisms. J Biol Chem 281:20567-20576
11. Jornvall H, Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D (1995) Short-chain dehydrogenases/reductases (SDR). Biochemistry 34:6003-6013
12. Kobori T, Sasaki H, Lee WC, Zenno S, Saigo K, Murphy ME, Tanokura M (2001) Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution. J Biol Chem 276:2816-2823
13. Liger D, Graille M, Zhou CZ, Leulliot N, Quevillon-Cheruel S, Blondeau K, Janin J, van Tilbeurgh H (2004) Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities. J Biol Chem 279:34890-34897
14. Liu G, Zhou J, Lv H, Xiang X, Wang J, Zhou M, Qv Y (2007a) Azoreductase from Rhodobacter sphaeroides AS1.1737 is a flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase. Appl Microbiol Biotechnol 76:1271-1279
15. Liu ZJ, Chen H, Shaw N, Hopper SL, Chen L, Chen S, Cerniglia CE, Wang BC (2007b) Crystal structure of an aerobic FMN-dependent azoreductase (AzoA) from Enterococcus faecalis. Arch Biochem Biophys 463:68-77
16. Nakanishi M, Yatome C, Ishida N, Kitade Y (2001) Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase. J Biol Chem 276:46394-46399
17. Nicholas KB, Nicholas HB Jr, Deerfield DW II (1997) GeneDoc: analysis and visualization of genetic variation. EMBnet News 4:1-4
18. Raffi F, Hall JD, Cerniglia CE (1997) Mutagenicity of azo dyes used in foods, drugs and cosmetics before and after reduction by Clostridium species from the human intestinal tract. Food Chem Toxicol 35:897-901
19. Reyes VM, Sawaya MR, Brown KA, Kraut J (1995) Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications. Biochemistry 34:2710-2723
20. Shore J (1996) Advances in direct dyes. Ind J Fibre Text Res 21:1-29
21. Stolz A (2001) Basic and applied aspects in the microbial degradation of azo dyes. Appl Microbiol Biotechnol 56:69-80
22. Suzuki Y, Yoda T, Ruhul A, Sugiura W (2001) Molecular cloning and characterization of the gene coding for azoreductase from Bacillus sp. OY1-2 isolated from soil. J Biol Chem 276:9059-9065
23. Wang CJ, Hagemeier C, Rahman N, Lowe E, Noble M, Coughtrie M, Sim E, Westwood I (2007) Molecular cloning, characterization and ligand-bound structure of an azoreductase from Pseudomonas aeruginosa. J Mol Biol 373:1213-1228
24. Wilson DK, Bohren KM, Gabbay KH, Quiocho FA (1992) An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257:81-84
25. Yan B, Zhou J, Wang J, Du C, Hou H, Song Z, Bao Y (2004) Expression and characteristics of the gene encoding azoreductase from Rhodobacter sphaeroides AS1.1737. FEMS Microbiol Lett 236:129-136