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Volumn 194, Issue 8, 2012, Pages 2041-2049

Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids

Author keywords

[No Author keywords available]

Indexed keywords

1 METHYLXANTHINE; 3 METHYLXANTHINE; 7 METHYLXANTHINE; CAFFEINE; FLAVINE MONONUCLEOTIDE; N DEMETHYLASE; NDMA PROTEIN; NDMB PROTEIN; NDMD PROTEIN; PARAXANTHINE; PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; THEOBROMINE; THEOPHYLLINE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; XANTHINE;

EID: 84861211147     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06637-11     Document Type: Article
Times cited : (79)

References (34)
  • 1
    • 0037456369 scopus 로고    scopus 로고
    • Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA
    • Aas PA, et al. 2003. Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA. Nature 421:859-863.
    • (2003) Nature , vol.421 , pp. 859-863
    • Aas, P.A.1
  • 2
    • 77957585021 scopus 로고    scopus 로고
    • Pharmacokinetics and metabolism of natural methylxanthines in animal and man
    • Fredholm BB (ed), Springer-Verlag, Berlin, Germany
    • Arnaud MJ. 2011. Pharmacokinetics and metabolism of natural methylxanthines in animal and man, p 33-91. In Fredholm BB (ed), Handbook of experimental pharmacology, vol 200. Springer-Verlag, Berlin, Germany.
    • (2011) Handbook of experimental pharmacology , vol.200 , pp. 33-91
    • Arnaud, M.J.1
  • 3
    • 0002557598 scopus 로고
    • Phthalate dioxygenase reductase and related flavin-iron-sulfur containing electron transferases
    • Müller F (ed), CRC Press, Boca Raton, FL
    • Batie CJ, Ballou DP, Correll CC. 1991. Phthalate dioxygenase reductase and related flavin-iron-sulfur containing electron transferases, p 546- 566. In Müller F (ed), Chemistry and biochemistry of flavoenzymes, vol 3. CRC Press, Boca Raton, FL.
    • (1991) Chemistry and biochemistry of flavoenzymes , vol.3 , pp. 546-566
    • Batie, C.J.1    Ballou, D.P.2    Correll, C.C.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 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 -254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0023778061 scopus 로고
    • Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase
    • Brunel F, Davidson J. 1988. Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase. J. Bacteriol. 170:4924-4930.
    • (1988) J. Bacteriol. , vol.170 , pp. 4924-4930
    • Brunel, F.1    Davidson, J.2
  • 6
    • 77954129578 scopus 로고    scopus 로고
    • Overlap extension PCR cloning: a simple and reliable way to create recombinant plasmids
    • Bryksin AV, Matsumura I. 2010. Overlap extension PCR cloning: a simple and reliable way to create recombinant plasmids. Biotechniques 48: 463-465.
    • (2010) Biotechniques , vol.48 , pp. 463-465
    • Bryksin, A.V.1    Matsumura, I.2
  • 7
    • 33746731093 scopus 로고    scopus 로고
    • Combined sewer overflows to surface waters detected by the anthropogenic marker caffeine
    • Buerge IJ, Poiger T, Muller MD, Buser HR. 2006. Combined sewer overflows to surface waters detected by the anthropogenic marker caffeine. Environ. Sci. Technol. 40:4096-4102.
    • (2006) Environ. Sci. Technol. , vol.40 , pp. 4096-4102
    • Buerge, I.J.1    Poiger, T.2    Muller, M.D.3    Buser, H.R.4
  • 8
    • 33845314714 scopus 로고    scopus 로고
    • Catabolic pathways and biotechnological applications of microbial caffeine degradation
    • Dash SS, Gummadi SN. 2006. Catabolic pathways and biotechnological applications of microbial caffeine degradation. Biotechnol. Lett. 28:1993- 2002.
    • (2006) Biotechnol. Lett. , vol.28 , pp. 1993-2002
    • Dash, S.S.1    Gummadi, S.N.2
  • 10
    • 69049107348 scopus 로고    scopus 로고
    • Crystal structure of dicamba monooxygenase: a Rieske nonheme oxygenase that catalyzes oxidative demethylation
    • Dumitru R, Wang WZ, Weeks DP, Wilson MA. 2009. Crystal structure of dicamba monooxygenase: a Rieske nonheme oxygenase that catalyzes oxidative demethylation. J. Mol. Biol. 392:498 -510.
    • (2009) J. Mol. Biol. , vol.392 , pp. 498-510
    • Dumitru, R.1    Wang, W.Z.2    Weeks, D.P.3    Wilson, M.A.4
  • 12
    • 36749041363 scopus 로고    scopus 로고
    • The obesity-associated FTO gene encodes a 2-oxoglutarate-dependent nucleic acid demethylase
    • Gerken T, et al. 2007. The obesity-associated FTO gene encodes a 2-oxoglutarate-dependent nucleic acid demethylase. Science 318:1469 -1472.
    • (2007) Science , vol.318 , pp. 1469-1472
    • Gerken, T.1
  • 13
    • 0034029015 scopus 로고    scopus 로고
    • Aromatic hydrocarbon dioxygenases in environmental biotechnology
    • Gibson DT, Parales RE. 2000. Aromatic hydrocarbon dioxygenases in environmental biotechnology. Curr. Opin. Biotechnol. 11:236 -243.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 236-243
    • Gibson, D.T.1    Parales, R.E.2
  • 14
    • 78649505567 scopus 로고    scopus 로고
    • Biochemistry and occurrence of Odemethylation in plant metabolism
    • Hagel JM, Facchini PJ. 2010. Biochemistry and occurrence of Odemethylation in plant metabolism. Front. Physiol. 1:14.
    • (2010) Front. Physiol. , vol.1 , pp. 14
    • Hagel, J.M.1    Facchini, P.J.2
  • 15
    • 0025055440 scopus 로고
    • Purifcation and properties of NADHferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816
    • Haigler BE, Gibson DT. 1990. Purifcation and properties of NADHferredoxinNAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816. J. Bacteriol. 172:457- 464.
    • (1990) J. Bacteriol. , vol.172 , pp. 457-464
    • Haigler, B.E.1    Gibson, D.T.2
  • 16
    • 21644451831 scopus 로고    scopus 로고
    • A three-component dicamba O-demethylase from Pseudomonas maltophilia, strain DI-6: gene isolation, characterization, and heterologous expression
    • Herman PL, et al. 2005. A three-component dicamba O-demethylase from Pseudomonas maltophilia, strain DI-6: gene isolation, characterization, and heterologous expression. J. Biol. Chem. 280:24759 -24767.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24759-24767
    • Herman, P.L.1
  • 17
    • 0026527083 scopus 로고
    • Mechanisms of cytochrome P450 and peroxidasecatalyzed xenobiotic metabolism
    • Hollenberg PF. 1992. Mechanisms of cytochrome P450 and peroxidasecatalyzed xenobiotic metabolism. FASEB J. 6:686-694.
    • (1992) FASEB J , vol.6 , pp. 686-694
    • Hollenberg, P.F.1
  • 18
    • 0033567453 scopus 로고    scopus 로고
    • Determination of submicromolar concentrations of formaldehyde by liquid chromatography
    • Jones SB, Terry CM, Lister TE, Johnson DC. 1999. Determination of submicromolar concentrations of formaldehyde by liquid chromatography. Anal. Chem. 71:4030-4033.
    • (1999) Anal. Chem. , vol.71 , pp. 4030-4033
    • Jones, S.B.1    Terry, C.M.2    Lister, T.E.3    Johnson, D.C.4
  • 20
    • 43149093388 scopus 로고    scopus 로고
    • A new classification system for bacterial Rieske non-heme iron aromatic ring-hydroxylating oxygenases
    • Kweon O, et al. 2008. A new classification system for bacterial Rieske non-heme iron aromatic ring-hydroxylating oxygenases. BMC Biochem. 9:11.
    • (2008) BMC Biochem , vol.9 , pp. 11
    • Kweon, O.1
  • 21
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2 0
    • Larkin MA, et al. 2007. Clustal W and Clustal X version 2.0. Bioinformatics 23:2947-2948.
    • (2007) Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1
  • 23
    • 0032519353 scopus 로고    scopus 로고
    • GeneMark.hmm: new solutions for gene finding
    • Lukashin AV, Borodovsky M. 1998. GeneMark.hmm: new solutions for gene finding. Nucleic Acids Res. 26:1107-1115.
    • (1998) Nucleic Acids Res , vol.26 , pp. 1107-1115
    • Lukashin, A.V.1    Borodovsky, M.2
  • 25
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 27
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi Y, et al. 2004. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119:941-953.
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1
  • 28
    • 0018790274 scopus 로고
    • Toluene dioxygenase: purification of an iron-sulfur protein by affinity chromatography
    • Subramanian V, Liu T, Yeh W, Gibson DT. 1979. Toluene dioxygenase: purification of an iron-sulfur protein by affinity chromatography. Biochem. Biophys. Res. Commun. 91:1131-1139.
    • (1979) Biochem. Biophys. Res. Commun. , vol.91 , pp. 1131-1139
    • Subramanian, V.1    Liu, T.2    Yeh, W.3    Gibson, D.T.4
  • 30
    • 79951486835 scopus 로고    scopus 로고
    • Characterization of a broad-specificity non-haem ironN-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source
    • Summers RM, Louie TM, Yu CL, Subramanian M. 2011. Characterization of a broad-specificity non-haem ironN-demethylase from Pseudomonas putida CBB5 capable of utilizing several purine alkaloids as sole carbon and nitrogen source. Microbiology 157:583-592.
    • (2011) Microbiology , vol.157 , pp. 583-592
    • Summers, R.M.1    Louie, T.M.2    Yu, C.L.3    Subramanian, M.4
  • 31
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • Tsukada Y, et al. 2006. Histone demethylation by a family of JmjC domain-containing proteins. Nature 439:811- 816.
    • (2006) Nature , vol.439 , pp. 811-816
    • Tsukada, Y.1
  • 32
    • 0015500791 scopus 로고
    • Enzymatic ω-oxidation VI. Isolation of homogenous reduced diphosphopyridine nucleotide-rubredoxin reductase
    • Ueda T, Lode ET, Coon MJ. 1972. Enzymatic ω-oxidation. VI. Isolation of homogenous reduced diphosphopyridine nucleotide-rubredoxin reductase. J. Biol. Chem. 247:2109 -2116.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2109-2116
    • Ueda, T.1    Lode, E.T.2    Coon, M.J.3
  • 33
    • 33947194500 scopus 로고    scopus 로고
    • Purification, characterization, and crystallization of the components of a biphenyl dioxygenase system from Sphingobium yanoikuyae B1
    • Yu CL, et al. 2007. Purification, characterization, and crystallization of the components of a biphenyl dioxygenase system from Sphingobium yanoikuyae B1. J. Ind. Microbiol. Biotechnol. 34:311-324.
    • (2007) J. Ind. Microbiol. Biotechnol. , vol.34 , pp. 311-324
    • Yu, C.L.1
  • 34
    • 67650337822 scopus 로고    scopus 로고
    • Two distinct pathways for metabolism of theophylline and caffeine are coexpressed in Pseudomonas putida CBB5
    • Yu CL, et al. 2009. Two distinct pathways for metabolism of theophylline and caffeine are coexpressed in Pseudomonas putida CBB5. J. Bacteriol. 191:4624-4632.
    • (2009) J. Bacteriol. , vol.191 , pp. 4624-4632
    • Yu, C.L.1


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