Biodegradation of phenanthrene by Pseudomonas sp. strain PPD: Purification and characterization of 1-hydroxy-2-naphthoic acid dioxygenase

Microbiology

Volumn 155, Issue 9, 2009, Pages 3083-3091

  Deveryshetty, Jaigeeth ^a   Phale, Prashant S ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

1 HYDROXY 2 NAPHTHOIC ACID DIOXYGENASE; 2 CARBOXYBENZALPYRUVIC ACID; 2 NAPHTHOIC ACID DERIVATIVE; 3 HYDROXY 2 NAPHTHOIC ACID; AROMATIC CARBOXYLIC ACID; DIOXYGENASE; GENTISIC ACID; HYDROXYNAPHTHOIC ACID; IRON; PHENANTHRENE; PYRUVIC ACID DERIVATIVE; SALICYLIC ACID; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL METABOLISM; BIODEGRADATION; COMPETITIVE INHIBITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; MOLECULAR WEIGHT; NONHUMAN; PH; PRIORITY JOURNAL; PSEUDOMONAS; SIGNAL TRANSDUCTION; STOICHIOMETRY;

BACTERIAL PROTEINS; BIOTRANSFORMATION; CHELATING AGENTS; DIOXYGENASES; EDETIC ACID; EGTAZIC ACID; ENZYME ACTIVATION; METABOLIC NETWORKS AND PATHWAYS; NAPHTHOLS; PHENANTHRENES; PSEUDOMONAS; SUBSTRATE SPECIFICITY;

PSEUDOMONAS SP.;

EID: 69949156904     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.030460-0     Document Type: Article

References (40)

1. Adachi, K., Iwayama, Y., Taniok, H. & Takeda, Y. (1966). Purification and properties of homogentisate oxygenase from Pseudomonas fluorescens. Biochim Biophys Acta 118, 88-97.
2. Adachi, K., Iwabuchi, T., Sano, H. & Harayama, S. (1999). Structure of the ring cleavage product of 1-hydroxy-2-naphthoate, an intermediate of the phenanthrene-degradative pathway of Nocardioides sp. strain KP7. J Bacteriol 181, 757-763.
3. Adams, M. A., Singh, V. K., Keller, B. O. & Jia, Z. (2006). Structural and biochemical characterization of gentisate 1,2-dioxygenase from Escherichia coli O157 : H7. Mol Microbiol 61, 1469-1484.
4. 2+ of extradiol dioxygenases. J Biol Chem 261, 2170-2178.
5. Barnsley, E. A. (1983). Phthalate pathway of phenanthrene metabolism: formation of 2′-carboxybenzalpyruvate. J Bacteriol 154, 113-117.
6. Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
7. Bucker, M., Glatt, H. R., Platt, K. L., Avnir, D., Ittah, Y., Blum, J. & Oesch, F. (1979). Mutagenicity of phenanthrene and phenanthrene K-region derivatives. Mutat Res 66, 337-348.
8. Chang, H. K. & Zylstra, G. J. (1999). Characterization of the phthalate permease OphD from Burkholderia cepacia ATCC 17616. J Bacteriol 181, 6197-6199.
9. Crawford, R. L., Hutton, S. W. & Chapman, P. J. (1975). Purification and properties of gentisate 1,2-dioxygenase from Moraxella osloensis. J Bacteriol 121, 794-799.
10. Davis, M. I., Orville, A. M., Neese, F., Zaleski, J. M., Lipscomb, J. D. & Solomon, E. I. (2002). Spectroscopic and electronic structure studies of protocatechuate 3,4-dioxygenase: nature of tyrosinate-Fe(III) bonds and their contribution to reactivity. J Am Chem Soc 124, 602-614.
11. Deveryshetty, J., Suvekbala, V., Varadamshetty, G. & Phale, P. S. (2007). Metabolism of 2-, 3- and 4-hydroxybenzoates by soil isolates Alcaligenes sp. strain PPH and Pseudomonas sp. strain PPD. FEMS Microbiol Lett 268, 59-66.
12. Doddamani, H. P. & Ninnekar, H. Z. (2000). Biodegradation of phenanthrene by a Bacillus species. Curr Microbiol 41, 11-14.
13. Evans, W. C., Fernley, H. N. & Griffiths, E. (1965). Oxidative metabolism of phenanthrene and anthracene by soil pseudomonads. The ring-fission mechanism. Biochem J 95, 819-831.
14. Feng, Y., Khoo, H. E. & Poh, C. L. (1999). Purification and characterization of gentisate 1,2-dioxygenases from Pseudomonas alcaligenes NCIB 9867 and Pseudomonas putida NCIB 9869. Appl Environ Microbiol 65, 946-950.
15. Ghosh, D. K. & Mishra, A. K. (1983). Oxidation of phenanthrene by a strain of Micrococcus: evidence of protocatechuate pathway. Curr Microbiol 9, 219-224.
16. Harpel, M. R. & Lipscomb, J. D. (1990). Gentisate 1,2-dioxygenase from Pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans. J Biol Chem 265, 6301-6311.
17. Hayaishi, O. & Hoshimoto, K. (1950). Pyrocatecase, a new enzyme catalyzing oxidative breakdown of pyrocatechin. J Biochem 37, 371-374.
18. Hintner, J. P., Lechner, C., Riegert, U., Kuhm, A. E., Storm, T., Reemtsma, T. & Stolz, A. (2001). Direct ring fission of salicylate by a salicylate 1,2-dioxygenase activity from Pseudaminobacter salicylatoxidans. J Bacteriol 183, 6936-6942.
19. Hintner, J. P., Reemtsma, T. & Stolz, A. (2004). Biochemical and molecular characterization of a ring fission dioxygenase with the ability to oxidize (substituted) salicylate(s) from Pseudaminobacter salicylatoxidans. J Biol Chem 279, 37250-37260.
20. Iwabuchi, T. & Harayama, S. (1997). Biochemical and genetic characterization of 2-carboxybenzaldehyde dehydrogenase, an enzyme involved in phenanthrene degradation by Nocardioides sp. strain KP7. J Bacteriol 179, 6488-6494.
21. Iwabuchi, T. & Harayama, S. (1998). Biochemical and molecular characterization of 1-hydroxy-2-naphthoate dioxygenase from Nocardioides sp. KP7. J Biol Chem 273, 8332-8336.
22. Kita, A., Kita, S., Fujisawa, I., Inaka, K., Ishida, T., Horiike, K., Nozaki, M. & Miki, K. (1999). An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2. Structure 7, 25-34.
23. Kiyohara, H., Nagao, K. & Nomi, R. (1976). Degradation of phenanthrene through o-phthalate by an Aeromonas sp. Agric Biol Chem 40, 1075-1082.
24. Kojima, Y., Itada, N. & Hayaishi, O. (1961). Metapyrocatachase: a new catechol-cleaving enzyme. J Biol Chem 236, 2223-2228.
25. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
26. March, S. C., Parikh, I. & Cuatrecasas, P. (1974). A simplified method for cyanogen bromide activation of agarose for affinity chromatography. Anal Biochem 60, 149-152.
27. Mastrangelo, G., Fadda, E. & Marzia, V. (1996). Polycyclic aromatic hydrocarbons and cancer in man. Environ Health Perspect 104, 1166-1170.
28. Matera, I., Ferraroni, M., Burger, S., Scozzafava, A., Stolz, A. & Briganti, F. (2008). Salicylate 1,2-dioxygenase from Pseudaminobacter salicylatoxidans: crystal structure of a peculiar ring-cleaving dioxygenase. J Mol Biol 380, 856-868.
29. Ono, K., Nozaki, M. & Hayaishi, O. (1970). Purification and some properties of protocatechuate 4,5-dioxygenase. Biochim Biophys Acta 220, 224-238.
30. Phale, P. S., Basu, A., Majhi, P. D., Deveryshetty, J., Vamsee-Krishna, C. & Shrivastava, R. (2007). Metabolic diversity in bacterial degradation of aromatic compounds. OMICS 11, 252-279.
31. Prabhu, Y. & Phale, P. S. (2003). Biodegradation of phenanthrene by Pseudomonas sp. strain PP2: novel metabolic pathway, role of biosurfactant and cell surface hydrophobicity in hydrocarbon assimilation. Appl Microbiol Biotechnol 61, 342-351.
32. Samanta, S. K., Chakraborti, A. K. & Jain, R. K. (1999). Degradation of phenanthrene by different bacteria: evidence for novel transformation sequences involving the formation of 1-naphthol. Appl Microbiol Biotechnol 53, 98-107.
33. Shu, L., Chiou, Y. M., Orville, A. M., Miller, M. A., Lipscomb, J. D. & Que, L., Jr (1995). X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism. Biochemistry 34, 6649-6659.
34. Stanier, R. Y. & Ingraham, J. L. (1954). Protocatechuic acid oxidase. J Biol Chem 210, 799-808.
35. Sugumaran, M. & Vaidyanathan, C. S. (1978). Affinity chromatography of homogentisate 1,2-dioxygenase from Aspegillus niger. FEMS Microbiol Lett 4, 343-347.
36. Vamsee-Krishna, C. & Phale, P. S. (2008). Bacterial degradation of phthalate isomers and their esters. Indian J Microbiol 48, 19-34.
37. Vamsee-Krishna, C., Mohan, Y. & Phale, P. S. (2006). Biodegradation of phthalate isomers by Pseudomonas aeruginosa PP4, Pseudomonas sp. PPD and Acinetobacter lwoffii ISP4. Appl Microbiol Biotechnol 72, 1263-1269.
38. Vetting, M. W. & Ohlendorf, D. H. (2000). The 1.8 Å crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker. Structure 8, 429-440.
39. Vetting, M. W., D'Argenio, D. A., Ornston, L. N. & Ohlendorf, D. H. (2000). Structure of Acinetobacter strain ADP1 protocatechuate 3, 4-dioxygenase at 2.2 Å resolution: implications for the mechanism of an intradiol dioxygenase. Biochemistry 39, 7943-7955.
40. Werwath, J., Arfmann, H. A., Pieper, D. H., Timmis, K. N. & Wittich, R. M. (1998). Biochemical and genetic characterization of a gentisate 1,2-dioxygenase from Sphingomonas sp. strain RW5. J Bacteriol 180, 4171-4176.