메뉴 건너뛰기




Volumn 1, Issue 3-4, 2008, Pages 225-230

Isolation of cytoplasmic NADPH-dependent phenol hydroxylase and catechol-1,2-dioxygenase from Candida tropicalis yeast

Author keywords

biodegradation; Candida tropicalis; catechol 1,2 dioxygenase; environmental pollutants; NADPH dependent phenol hydroxylase; phenol; yeast

Indexed keywords


EID: 77349089089     PISSN: 13376853     EISSN: 13379569     Source Type: Journal    
DOI: 10.2478/v10102-010-0046-7     Document Type: Article
Times cited : (10)

References (28)
  • 3
    • 0015594073 scopus 로고
    • Metabolism of phenol and cresols by mutants of Pseudomonas putida.
    • Bayly RC, Wigmore GJ. (1973) Metabolism of phenol and cresols by mutants of Pseudomonas putida. J Bacteriol 113: 1112-1120.
    • (1973) J Bacteriol , vol.113 , pp. 1112-1120
    • Bayly, R.C.1    Wigmore, G.J.2
  • 4
    • 0030809197 scopus 로고    scopus 로고
    • Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens.
    • Briganti F, Pessione E, Guinta C, Scozzafava A. (1997) Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens. FEBS Lett 416: 61-64.
    • (1997) FEBS Lett , vol.416 , pp. 61-64
    • Briganti, F.1    Pessione, E.2    Guinta, C.3    Scozzafava, A.4
  • 5
    • 0032487754 scopus 로고    scopus 로고
    • Batch phenol degradation by Candida tropicalis and its fusant.
    • Chang YH, Li CT, Chang MC, Shieh WK. (1998) Batch phenol degradation by Candida tropicalis and its fusant. Biotechnol Bioeng 60: 391-395.
    • (1998) Biotechnol Bioeng , vol.60 , pp. 391-395
    • Chang, Y.H.1    Li, C.T.2    Chang, M.C.3    Shieh, W.K.4
  • 6
    • 0027391396 scopus 로고
    • Bettler J Cloning and characterization of a gene coding for the catechol 1,2-dioxygenase of Acinetobacter sp. mA3.
    • Eck R, Bettler J (1991) Cloning and characterization of a gene coding for the catechol 1,2-dioxygenase of Acinetobacter sp. mA3. Gene 123: 87-92.
    • (1991) Gene , vol.123 , pp. 87-92
    • Eck, R.1
  • 7
    • 0024507346 scopus 로고
    • Isolation of phenol-degradation Bacillus stearothermophilus and partial characterization of phenol hydroxylase.
    • Gurujeyalakshmi G, Oriel P. (1989) Isolation of phenol-degradation Bacillus stearothermophilus and partial characterization of phenol hydroxylase. Appl Environ Microbio. 55: 500-502
    • (1989) Appl Environ Microbio. , vol.55 , pp. 500-502
    • Gurujeyalakshmi, G.1    Oriel, P.2
  • 8
    • 4243899561 scopus 로고    scopus 로고
    • Kinetics of phenol oxidation by Candida tropicalis yeast (in Czech).
    • Komárková E, Páca J. (2000) Kinetics of phenol oxidation by Candida tropicalis yeast (in Czech). Chem Listy 94: 729.
    • (2000) Chem Listy , vol.94 , pp. 729
    • Komárková, E.1    Páca, J.2
  • 10
    • 0021815526 scopus 로고
    • Degradation of phenolic compounds by yeast Candida tropicalis HP15. I. Physiology of growth and substrate utilization.
    • Krug M, Ziegler H, Straube G. (1985) Degradation of phenolic compounds by yeast Candida tropicalis HP15. I. Physiology of growth and substrate utilization. J Basic Microbiol 2: 102-110.
    • (1985) J Basic Microbiol , vol.2 , pp. 102-110
    • Krug, M.1    Ziegler, H.2    Straube, G.3
  • 11
    • 0022962816 scopus 로고
    • Degradation of phenolic compounds by yeast Candida tropicalis HP15. II. Some properties of the first two enzymes of the degradation pathway.
    • Krug M, Straube G. (1986) Degradation of phenolic compounds by yeast Candida tropicalis HP15. II. Some properties of the first two enzymes of the degradation pathway. J Basic Microbiol 5: 271-281.
    • (1986) J Basic Microbiol , vol.5 , pp. 271-281
    • Krug, M.1    Straube, G.2
  • 12
    • 0004412275 scopus 로고    scopus 로고
    • Inhibition concentration of phenolic substances under different cultivation conditions. Part II. Impact of dissolved oxygen concentration and temperature on degradation kinetics.
    • Martius GGS, Stottmeister U, Jechorek M, Páca J. (1996) Inhibition concentration of phenolic substances under different cultivation conditions. Part II. Impact of dissolved oxygen concentration and temperature on degradation kinetics. Acta Hydrochim Hydrobiol 24: 168-175.
    • (1996) Acta Hydrochim Hydrobiol , vol.24 , pp. 168-175
    • Martius, G.G.S.1    Stottmeister, U.2    Jechorek, M.3    Páca, J.4
  • 13
    • 0025159432 scopus 로고
    • Three isoenzymes of catechol 1,2-dioxygenase (pyrocatechase), aa, aβ, and ββ, from Pseudomonas arvilla C-1.
    • Nakai C, Horiike K, Kuramitsu S, Kagamiyama H, Nozaki M, (1990) Three isoenzymes of catechol 1,2-dioxygenase (pyrocatechase), aa, aβ, and ββ, from Pseudomonas arvilla C-1. J Biol Chem 265: 660-665.
    • (1990) J Biol Chem , vol.265 , pp. 660-665
    • Nakai, C.1    Horiike, K.2    Kuramitsu, S.3    Kagamiyama, H.4    Nozaki, M.5
  • 14
    • 0015790898 scopus 로고
    • Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporum cutaneum.
    • Neujahr HY, Gaal A. (1973) Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporum cutaneum. Eur J Biochem 35: 386-400.
    • (1973) Eur J Biochem , vol.35 , pp. 386-400
    • Neujahr, H.Y.1    Gaal, A.2
  • 15
    • 0037516742 scopus 로고    scopus 로고
    • Kinetics of phenol oxidation by Candida tropicalis: effects of oxygen supply rate and nutrients on phenol inhibition.
    • Páca J, Komárková E, Prell A, Stiborová M, Sobotka M. (2002) Kinetics of phenol oxidation by Candida tropicalis: effects of oxygen supply rate and nutrients on phenol inhibition. Folia Microbiol 47: 685-692.
    • (2002) Folia Microbiol , vol.47 , pp. 685-692
    • Páca, J.1    Komárková, E.2    Prell, A.3    Stiborová, M.4    Sobotka, M.5
  • 16
    • 33847329090 scopus 로고    scopus 로고
    • Isolation and partial characterization of cytoplasmic NADPHdependent phenol hydroxylase oxidizing phenol to catechol in Candida tropicalis yeast.
    • Páca J Jr, Kremlácková V, Turek M, Suchá V, Vilímková L, Páca J, Halecký M, Stiborová M, (2007) Isolation and partial characterization of cytoplasmic NADPHdependent phenol hydroxylase oxidizing phenol to catechol in Candida tropicalis yeast. Enzyme Microb Tech 40: 919-926.
    • (2007) Enzyme Microb Tech , vol.40 , pp. 919-926
    • Páca, J.1    Kremlácková, V.2    Turek, M.3    Suchá, V.4    Vilímková, L.5    Páca, J.6    Halecký, M.7    Stiborová, M.8
  • 17
    • 0001348251 scopus 로고    scopus 로고
    • Inhibition concentration of phenolic substances under different cultivation conditions. Part I. Phenol oxidation by mixed microbial population in a model system.
    • Páca J, Martius GGS. (1996) Inhibition concentration of phenolic substances under different cultivation conditions. Part I. Phenol oxidation by mixed microbial population in a model system. Acta Hydrochim Hydrobiol 24: 127-131.
    • (1996) Acta Hydrochim Hydrobiol , vol.24 , pp. 127-131
    • Páca, J.1    Martius, G.G.S.2
  • 18
    • 1842810904 scopus 로고    scopus 로고
    • Functional identification of the gene locus (ncg12319) and characterization of catechol 1,2-dioxygenase in Corybebacterium glutamicum.
    • Shen XH, Liu ZP, Liu SJ. (2004) Functional identification of the gene locus (ncg12319) and characterization of catechol 1,2-dioxygenase in Corybebacterium glutamicum. Biotechnol Lett 26: 575-580.
    • (2004) Biotechnol Lett , vol.26 , pp. 575-580
    • Shen, X.H.1    Liu, Z.P.2    Liu, S.J.3
  • 19
    • 0025250503 scopus 로고
    • Substrate inhibition of phenol oxidation by a strain of Candida tropicalis.
    • Stephenson T. (1990) Substrate inhibition of phenol oxidation by a strain of Candida tropicalis. Biotechn Lett 12: 843-846.
    • (1990) Biotechn Lett , vol.12 , pp. 843-846
    • Stephenson, T.1
  • 20
    • 0029007323 scopus 로고
    • Benzenediazonium ion derived from Sudan I forms an 8-(phenylazo)guanine adduct in DNA.
    • Stiborová M, Asfaw B, Frei E, Schmeiser HH, Wiessler M. (1995) Benzenediazonium ion derived from Sudan I forms an 8-(phenylazo)guanine adduct in DNA. Chem Res Toxicol 8: 489-498.
    • (1995) Chem Res Toxicol , vol.8 , pp. 489-498
    • Stiborová, M.1    Asfaw, B.2    Frei, E.3    Schmeiser, H.H.4    Wiessler, M.5
  • 21
    • 0034861029 scopus 로고    scopus 로고
    • Human enzymes involved in metabolic activation of carcinogenic aristolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A2.
    • Stiborová M, Frei E, Wiessler M, Schmeiser HH. (2001a) Human enzymes involved in metabolic activation of carcinogenic aristolochic acids: evidence for reductive activation by cytochromes P450 1A1 and 1A2. Chem Res Toxicol 14: 1128-1137.
    • (2001) Chem Res Toxicol , vol.14 , pp. 1128-1137
    • Stiborová, M.1    Frei, E.2    Wiessler, M.3    Schmeiser, H.H.4
  • 22
    • 0035613227 scopus 로고    scopus 로고
    • Isolation of DT-diaphorase [NAD(P)H dehydrogenase (quinone)] from rat liver cytosol: identification of new substrates, carcinogenic aristolochic acids.
    • Stiborová M, Hájek M, Vošmiková H, Frei E, Schmeiser HH. (2001b) Isolation of DT-diaphorase [NAD(P)H dehydrogenase (quinone)] from rat liver cytosol: identification of new substrates, carcinogenic aristolochic acids. Collect Czech Chem Commun 66: 959-972.
    • (2001) Collect Czech Chem Commun , vol.66 , pp. 959-972
    • Stiborová, M.1    Hájek, M.2    Vošmiková, H.3    Frei, E.4    Schmeiser, H.H.5
  • 23
    • 8844286849 scopus 로고    scopus 로고
    • Study of enzymes metabolizing environmental pollutants as a means of modulating their biodegradation (in Czech).
    • Stiborová M, Hudecek J, Páca J Jr, Martínek V, Páca J. (2004) Study of enzymes metabolizing environmental pollutants as a means of modulating their biodegradation (in Czech). Chem Listy 98: 876-890.
    • (2004) Chem Listy , vol.98 , pp. 876-890
    • Stiborová, M.1    Hudecek, J.2    Páca, J.3    Martínek, V.4    Páca, J.5
  • 24
    • 0142155619 scopus 로고    scopus 로고
    • Hydroxylation of phenol to catechol by Candida tropicalis: involvement of cytochrome P450.
    • Stiborová M, Suchá V, Mikšanová M, Páca J Jr, Páca J. (2003) Hydroxylation of phenol to catechol by Candida tropicalis: involvement of cytochrome P450. Gen Physiol Biophys 22: 167-179.
    • (2003) Gen Physiol Biophys , vol.22 , pp. 167-179
    • Stiborová, M.1    Suchá, V.2    Mikšanová, M.3    Páca, J.4    Páca, J.5
  • 25
    • 33847126079 scopus 로고    scopus 로고
    • Purification and characterization of a catochel 1,2-dioxygenase from a phenol degrading Candida albicans TL3.
    • Tsai S-C, Li Y-K. (2007) Purification and characterization of a catochel 1,2-dioxygenase from a phenol degrading Candida albicans TL3. Arch Microbiol 187: 199-206.
    • (2007) Arch Microbiol , vol.187 , pp. 199-206
    • Tsai, S.-C.1    Li, Y.-K.2
  • 26
    • 29344453377 scopus 로고    scopus 로고
    • An isolated Candida albicans TL3 capable of degrading phenol at large concentration.
    • Tsai S-C, Tsai L-D, Li Y-K. (2005) An isolated Candida albicans TL3 capable of degrading phenol at large concentration. Biosci Biotechnol Biochem 69: 2358-2367.
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 2358-2367
    • Tsai, S.-C.1    Tsai, L.-D.2    Li, Y.-K.3
  • 27
    • 0016786772 scopus 로고
    • Dynamic and steady state studies of phenol biodegradation in pure and mixed cultures.
    • Yang R, Humphrey AE. (1975) Dynamic and steady state studies of phenol biodegradation in pure and mixed cultures. Biotechno. Bioeng 17: 1211-1235.
    • (1975) Biotechno. Bioeng , vol.17 , pp. 1211-1235
    • Yang, R.1    Humphrey, A.E.2
  • 28
    • 0035900019 scopus 로고    scopus 로고
    • Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met.
    • Xu D, Ballou DP, Massey V. (2001) Studies of the mechanism of phenol hydroxylase: mutants Tyr289Phe, Asp54Asn, and Arg281Met. Biochemistry 40: 12369-12378.
    • (2001) Biochemistry , vol.40 , pp. 12369-12378
    • Xu, D.1    Ballou, D.P.2    Massey, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.