PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2012 | 59 | 3 |

Tytuł artykułu

Characterization of catechol 2,3-dioxygenase from Planococcus sp. strain S5 induced by high phenol concentration

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
 This study aimed at characterization of a new catechol 2,3-dioxygenase isolated from a Gram-positive bacterium able to utilize phenol as the sole carbon and energy source. Planococcus sp. strain S5 grown on 1 or 2 mM phenol showed activity of both a catechol 1,2- and catechol 2,3-dioxygenase while at a higher concentrations of phenol only catechol 2,3-dioxygenase activity was observed. The enzyme was optimally active at 60°C and pH 8.0. Kinetic studies showed that the Km and Vmax of the enzyme were 42.70 µM and 329.96 mU, respectively. The catechol 2,3-dioxygenase showed the following relative meta-cleavage activities for various catechols tested: catechol (100%), 3-methylcatechol (13.67%), 4-methylcatechol (106.33%) and 4-chlorocatechol (203.80%). The high reactivity of this enzyme towards 4-chlorocatechol is different from that observed for other catechol 2,3-dioxygenases. Nucleotide sequencing and homology search revealed that the gene encoding the S5 catechol 2,3-dioxygenase shared the greatest homology with the known genes encoding isoenzymes from Gram-negative Pseudomonas strains.

Wydawca

-

Rocznik

Tom

59

Numer

3

Opis fizyczny

p.345-351,fig.,ref.

Twórcy

  • Department of Biochemistry, Faculty of Biology and Environmental Protection, University of Silesia in Katowice, Katowice, Poland
autor

Bibliografia

  • Aneez Ahamad PYA, Kunhi AAM (1996) Degradation of phenol through orto-cleavage pathway by Pseudomonas stutzeri strain SPC2. Lett Appl Microbiol 45: 26-29.
  • Arai H, Ohishi T, Chang MY, Kudo T (2000) Arrangement and regulation of the genes for meta-pathway enzymes required for degradation of phenol in Comamonas testosteroni TA441. Microbiology 146: 1707-1715. 
  • Bae HS, Lee M, Kim JB, Lee ST (1996) Biodegradation of the mixtures of 4-chlorophenol and phenol by Comamonas testosteroni CPW301. Biodegradation 7: 463-469. 
  • Bartels I, Knackmuss HJ, Reineke W (1984) Suicide inactivation of catechol 2,3-dioxygenase from Pseudomonas putida mt-2 by 3-halocatechols. Appl Environ Microbiol 47: 500-505. 
  • Bayly RC, Dagley S, Gibson DT (1966) The metabolism of cresols by species of Pseudomonas. Biochem J 101: 293-301. 
  • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-58. 
  • Bugg TDH (2003) Dioxygenase enzymes: catalytic mechanisms and chemical models. Tetrahedron 59: 7075-101.
  • Bugg TD, Ramaswamy S (2008) Non-heme iron-dependent dioxygenases: unravelling catalytic mechanism for complex enzymatic oxidation. Curr Opin Chem Biol 12: 134-140. 
  • Candidus S, van Pee KH, Lingens F (1994) The catechol 2,3-dioxygenase gene of Rhodococcus rhodochrous CTM: nucleotide sequence, comparison with isofunctional dioxygenases and evidence for an active-site histidine. Microbiology 140: 321-330. 
  • Cao B, Geng A, Loh KC (2008) Induction of ortho- and meta- cleavage pathways in Pseudomonas in biodegradation of high benzoate concentration: MS identification of catabolic enzymes. Appl Microbiol Biotechnol 81: 99-107. 
  • Cerdan P, Rekik M, Harayama S (1995) Substrate specificity differences between two catechol 2,3-dioxygenases encoded by the TOL and NAH plasmids from Pseudomonas putida. Eur J Biochem 229: 113-118. 
  • Chae JC, Kim E, Bini E, Zylstra GJ (2007) Comparative analysis of the catechol 2,3-dioxygenase gene locus in thermoacidophilic Archeon Sulfolobus solfataricus strain 98/2. Biochem Biophys Res Commun 357: 815-819. 
  • Cho HJ, Kim K, Sohn SY, Cho HY, Kim KJ, Kim MH, Kim D, Kim E, Kang BS (2010) Substrate binding mechanism of a type I extradiol dioxygenase. J Biol Chem 285: 34643-34652. 
  • Chowdhury R, Sen AK, Karak P, Chatterjee R, Giri AK, Chaudhuri K. (2003) Isolation and characterization of an arsenic-resistant bacterium from a bore-well in West Bengal, India. Ann Microbiol 59: 253-258.
  • Dalal S, Panigrahi DP, Randhawa GS, Dubey RC (2012) Molecular characterization of high-strength polycyclic aromatic hydrocarbon (PAH)-degrading and phenol-tolerant bacteria obtained from thermal power plant wastewater. Chem Ecol DOI: 10.1080/02757540.2011.650166.
  • Djokic L, Narancic T, Nikodinovic-Runic J, Savic M, Vasiljevic B (2011a) Isolation and characterization of four novel Gram-positive bacteria associated with the rhizosphere of two endemorelict plants capable of degrading a broad range of aromatic substrates. Appl Microbiol Biotechnol 91: 1227-1238. 
  • Djokic L, Narancic T, Nikodinovic-Runic J, Bajkic S, Vasiljevic B (2011b) Four Bacillus sp. soil isolates capable of degrading phenol, toluene, biphenyl, naphthalene, and other aromatic compounds exhibit different aromatic catabolic potentials. Arch Biol Sci 63: 1057-1067.
  • Dong FM, Wang LL, Wang CM, Cheng JP, He ZQ, Sheng ZJ, Shen RQ (1992) Molecular cloning and mapping of phenol degradation genes from Bacillus stearothermophilus FTDP-3 and their expression in Escherichia coli. Appl Environ Microbiol 58: 2531-2535. 
  • Dong X, Hong Q, He L, Jiang X, Li S (2008) Characterization of phenol-degrading bacterial strains isolated from natural soil. Int Biodeterior Biodegradation 62: 257-262.
  • Duffner FM, Kirchner U, Bauer MP, Müller R (2000) Phenol/cresol degradation by the thermophilic Bacillus thermoglucosidansius A7: cloning and sequence analysis of five genes involved in the pathway. Gene 256: 215-221. 
  • Engelhardt MA, Daly K, Swannell RP, Head IM (2001) Isolation and characterization of a novel hydrocarbon-degrading, Gram-positive bacterium, isolated from intertidal beach sediment, and description of Planococcus alkanoclasticus sp. nov. J Appl Microbiol 90: 237-247. 
  • Feist CF, Hegeman GD (1969) Phenol and benzoate metabolism by Pseudomonas putida: regulation of tangential pathways. J Bacteriol 100: 869-877. 
  • Fortin P, Macpherson I, Neau D, Bolin J, Eltis L (2005) Directed evolution of a ring-cleaving dioxygenase for polychlorinated biphenyl degradation. J Biol Chem 280: 42307-42314. 
  • Harayama S, Rekik M (1989) Bacterial aromatic ring-cleavage enzymes are classified into two different gene families. J Biol Chem 264: 15328-15333. 
  • Hatta T, Mukerjee-Dhar G, Damborsky J, Kiyohara H, Kimbara K (2003) Characterization of a novel thermostable Mn(II)-dependent 2,3- dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8. J Biol Chem 278: 21483-21492. 
  • Hegeman GD (1966) Synthesis of the enzymes of the mandelate pathways by Pseudomonas putida. I. Synthesis of enzyme by the wild type. J Bacteriol 91: 1140-1150. 
  • Heinaru E, Truu J, Stottmeister U, Heinaru A (2000) Three types of phenol and p-cresol catabolism in phenol and p-cresol-degrading bacteria isolated from river water continuously polluted with phenolic compounds. FEMS Microbiol Ecol 31: 195-205. 
  • Hill KE, Fry JC, Weightman AJ (1994) Gene transfer in the aquatic environment: persistence and mobilization of the catabolic recombinant plasmid pDlO in the epilithon. Microbiology 140: 1555-1563.
  • Hugo N, Armengaud J, Gaillard J, Timmis KN, Jouanneau Y (1998) A novel -2FeS-2S-ferrodoxin from Pseudomonas putida mt2 promotes the reductive reactivation of catechols 2,3-dioxygenase. J Biol Chem 273: 9622-9629. 
  • Jacobucci DFC, Oriani MRG, Regina L (2009) Reducing COD level on oily effluent by utilizing biosurfactant-producing bacteria. Braz Arch Biol Technol 52: 1037-1042.
  • Jeong JJ, Kim JH, Kim CK, Hwang I, Lee K (2003) 3- and 4-alkylphenol degradation pathway in Pseudomonas sp. strain KL28: genetic organization of the lap gene cluster and substrate specificities of phenol hydroxylase and catechol 2,3-dioxygenase. Microbiology 149: 3265-3277. 
  • Jiang Y, Yang X, Liu B, Zhao H, Cheng Q, Cai B (2004) Catechol 2,3-dioxygenase from Pseudomonas sp. ND6. Gene sequence and enzyme characterization. Biosci Biotechnol Biochem 68: 1798-1800. 
  • Junca H, Plumeier I, Hecht HJ, Pieper DH (2004) Difference in kinetic behavior of catechol 2,3-dioxygenase variants from a polluted environment. Microbiology 150: 4181-4187. 
  • Jussila MM, Zhao J, Suominen L, Lindström K (2007) TOL plasmid transfer during bacterial conjugation in vitro and rhizoremediation of oil compounds in vivo. Environ Pollut 146: 510-524. 
  • Kalogeris E, Sanakis Y, Mamma D, Christakopoulos P, Kekos D, Stamatis H (2006) Properties of catechol 1,2-dioxygenase from Pseudomonas putida immobilized in calcium alginate hydrogels. Enzyme Microb Technol 39: 1113-1121.
  • Kasuga I, Nakajima F, Furumai H (2007) Diversity of catechol 2,3-dioxygenase genes of bacteria responding to dissolved organic matter derived from different sources in a eutrophic lake. FEMS Microbiol Ecol 61: 449-458. 
  • Kim D, Chae JC, Jang IY, Zylstra GJ, Kim YM, Kang BS, Kim EK (2005) Functional characterization and molecular modeling of methylcatechol 2,3-dioxygenase from o-xylene-degrading Rhodococcus sp. strain DK17. Biochem Biophys Res Commun 326: 880-886. 
  • Kim KP, Seo DI, Min KH, Ka JO, Park YK, Kim ChK (1997) Characteristics of catechol 2,3-dioxygenase produced by 4-chlorobenzoate-degrading Pseudomonas sp. S-47. J Microbiol 35: 295-299.
  • Klečka GM, Gibson DT (1981) Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol. Appl Environ Microbiol 41: 1159-1165. 
  • Łabużek S, Hupert-Kocurek K, Skurnik M (2003) Isolation and characterisation of new Planococcus sp. strain able for aromatic hydrocarbons degradation. Acta Microbiol Pol 52: 395-404. 
  • Li W, Shi J, Wang X, Han Y, Tong W, Ma L, Liu B, Cai B (2004) Complete nucleotide sequence and organization of the naphthalene catabolic plasmid pND6-1 from Pseudomonas sp. strain ND6. Gene 336: 231-240. 
  • Li H, Liu YH, Luo N, Zhang XY, Luan TG, Hu JM, Wang ZY, Wu PC, Chen MJ, Lu JQ (2006) Biodegradation of benzene and its derivatives by a psychrotolerant and moderately haloalkaliphilic Planococcus sp. strain ZD22. Res Microbiol 157: 629-636. 
  • Loh KC, Chua SS (2002) Ortho pathway of benzoate degradation in Pseudomonas putida: induction of meta pathway at high substrate concentrations. Enzyme Microb Technol 30: 620-626.
  • Lurie J, Rybnikova I (1986) Chemical analysis of industrial sewages. Gaschmizdat, Moscow (In Russian).
  • Ma H, Li G, Fang P, Zhang Y, Xu D (2010) Identification of phenol-degrading Nocardia sp. strain C-14-1 and characterization of its ring-cleavage 2,3-dioxygenase. Int J Biol 2: 79-83.
  • Milo RE, Duffner FM, Muller R (1999) Catechol 2,3-dioxygenase from the thermophilic, phenol-degrading Bacillus thermoleovorans strain A2 has unexpected low thermal stability. Extremophiles 3: 185-190. 
  • Müller Ch, Petruschka L, Cuypers H, Burchhardt G, Herrmann H (1996) Carbon catabolite repression of phenol degradation in Pseudomonas putidas mediated by the inhibition of the activator protein PhlR. J Bacteriol 178: 2030-2036. 
  • Murakami S, Nakanishi Y, Kodama N, Takenaka S, Shinke R, Aoki K (1998) Purification, characterization, and gene analysis of catechol 2,3- dioxygenase from the aniline- assimilating bacterium Pseudomonas species AW-2. Biosci Biotechnol Biochem 62: 747-752. 
  • Nakazawa T, Yokota T (1973) Benzoate metabolism in Pseudomonas putida (arvilla) mt-2: demonstration of two benzoate pathways. J Bacteriol 115: 262-267. 
  • Ng LC, Shingle V, Sze CC, Poh CL (1994) Cloning and sequences of the first eight genes of the chromosomally encoded (methyl) phenol degradation pathway from Pseudomonas putida P35X. Gene 151: 29-36. 
  • Nithya C, Gnanalakshmi B, Pandian SK (2011) Assessment and characterization of heavy metal resistance in Palk Bay sediment bacteria. Mar Environ Res 71: 283-294. 
  • Okuta A, Ohnishi K, Harayama S (1998) PCR isolation of catechol 2,3-dioxygenase gene fragments from environmental samples and their assembly into functional genes. Gene 212: 221-228. 
  • Palaniandavar M, Mayilmurugan R (2007) Mononuclear non-hem iron(III) complex as functional models for catechol dioxygenases. Comptes Rendus Chimie 10: 366-379.
  • Polissi A, Harayama S (1993) In vivo reactivation of catechol 2,3-dioxygenase mediated by a chloroplast-type ferredoxin: a bacterial strategy to expand the substrate specificity of aromatic degradative pathways. EMBO J 12: 3339-3347. 
  • Powlowski J, Shingler V (1994) Genetics and biochemistry of phenol degradation by Pseudomonas sp. CF600. Biodegradation 5: 219-236. 
  • Riegert U, Bürger S, Stolz A (2001) Altering catalytic properties of 3-chlorocatechol-oxidizing extradiol dioxygenase from Sphingomonas xenophaga BN6 by random mutagenesis. J Bacteriol 183: 2322-2330. 
  • Romano I, Giordano A, Lama L, Nicolaus B, Gambacorta A (2003) Planococcus rifietensis sp. nov, Isolated from Algal Mat Collected from a Sulfurous Spring in Campania (Italy). Syst Appl Microbiol 26: 357-366. 
  • Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: A laboratory manual. 2nd edn. Cold Spring Harbor Laboratory Press, New York.
  • Sato S, Nam JW, Kasuga K, Nojiri H, Yamane H, Omori T (1997) Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10. J Bacteriol 179: 4850-4858. 
  • Sei K, Asano K, Tateishi N, Mori K, Ike M, Fujita M (1999) Design of PCR primers and gene probes for the general detection of bacterial populations capable of degrading aromatic compounds via catechol cleavage pathways. J Biosci Bioeng 88: 542-550. 
  • Song J, Sung J, Kim YM, Zylstra GJ, Kim E (2000) Roles of the meta- and ortho-cleavage pathways for the efficient utilization of aromatic hydrocarbons by Sphingomonas yanoikuyae B1. J Microbiol 38: 245-249.
  • Sprott GD, Larocque S, Cadotte N, Dicaire CJ, McGee M, Brisson JR (2003) Novel polar lipids of halophilic eubacterium Planococcus H8 and archaeon Haloferax volcanii. Biochim Biophys Acta 1633: 179-188. 
  • Stillwell LC, Thurston SJ, Schneider RP, Romine MF, Fredrickson JK, Saffer JD (1995) Physical mapping and characterization of a catabolic plasmid from the deep-subsurface bacterium Sphingomonas sp. strain F199. J Bacteriol 177: 4537-4539. 
  • Takeo M, Nishimura M, Shirai M, Takahashi H, Negoro S (2007) Purification and characterization of catechol 2,3-dioxygenase from the aniline degradation pathway of Acinetobacter sp. YAA and its mutant enzyme, which resist substrate inhibition. Biosci Biotechnol Biochem 71: 1668-1675. 
  • Tancsics A, Szabó I, Baka E, Szoboszlay S, Kukolya J, Kriszt B, Marialigeti K (2010) Investigation of catechol 2,3-dioxygenase and 16S rRNA gene diversity in hypoxic, petroleum hydrocarbon contaminated groundwater. Syst Appl Microbiol 33: 398-406. 
  • Vaillancourt FH, Bolin JT, Eltis LD (2006) The ins and outs of ring-cleaving dioxygenases. Crit Rev Biochem Mol Biol 41: 241-67. 
  • Viggiani A, Siani L, Notomista E, Birolo L, Pucci P, Donato D (2004) The role of the conserved residues His-246, His-199, and Tyr-255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1. J Biol Chem 279: 48630-48639. 
  • Wallis M., Chapman S (1990) Isolation and partial characterization of an extradiol non-haem iron dioxygenase which preferentially cleaves 3-methylcatechol. Biochem J 266: 605-609. 
  • Wang Y, Xiao M, Geng X, Liu J, Chen J (2007) Horizontal transfer of genetic determinants for degradation of phenol between the bacteria living in plant and its rhizosphere. Appl Microbiol Biotechnol 77: 733-739. 
  • Wei J, Zhou Y, Xu T, Lu B, (2010) Rational design of catechol 2,3-dioxygenase for improving the enzyme characteristic. Appl Biochem Biotechnol 162: 116-126. 
  • Williams PA, Catterall FA, Murray K (1975) Metabolism of naphthalene, 2-methylnaphthalene, salicylate and benzoate by Pseudomonas PG: Regulation of tangential pathways. J Bacteriol 124: 679-685. 
  • Wojcieszyńska D, Hupert-Kocurek K, Greń I, Guzik U (2011) High activity catechols 2,3-dioxygenase from the cresols-degrading Stenotrophomonas maltophilia strain KB2. Int Biodeterior Biodegradation 65: 853-858.
  • Yrjälä K, Paulin L, Romantschuk M (1997) Novel oraganization of catechol meta-pathway genes in Sphingomonas sp. HV3 pSKY4 plasmid. FEMS Microbiol Lett 154: 403-408. 
  • Zou Y, Wei J, Jiang T, Gao W, Ma Y, Wei D (2007) Characterisation of thermostable catechol 2,3-dioxygenase from phenanthrene-degrading Pseudomonas sp. strain ZJF08. Ann Microbiol 57: 503-508.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-c9d381a5-8404-4a63-8503-fc21f1ede30d
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.