메뉴 건너뛰기




Volumn 195, Issue 17, 2013, Pages 3933-3939

Caffeine junkie: An unprecedented glutathione S-transferase-dependent oxygenase required for caffeine degradation by pseudomonas putida CBB5

Author keywords

[No Author keywords available]

Indexed keywords

7 METHYLXANTHINE; CAFFEINE; GLUTATHIONE S TRANSFERASE DEPENDENT RIESKE OXYGENASE; GLUTATHIONE TRANSFERASE; IRON SULFUR PROTEIN; NONHEME IRON PROTEIN; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; XANTHINE;

EID: 84883511622     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00585-13     Document Type: Article
Times cited : (29)

References (37)
  • 1
    • 37049181189 scopus 로고
    • Caffeine and related methylxanthines: possible naturally occurring pesticides
    • Nathanson JA. 1984. Caffeine and related methylxanthines: possible naturally occurring pesticides. Science 226:184-187.
    • (1984) Science , vol.226 , pp. 184-187
    • Nathanson, J.A.1
  • 3
    • 33646050615 scopus 로고    scopus 로고
    • Differential effect of selected methylxanthine derivatives on radiosensitization of lung carcinoma cells
    • Malki AM, Gentry J, Evans SC. 2006. Differential effect of selected methylxanthine derivatives on radiosensitization of lung carcinoma cells. Exp. Oncol. 28:16-24.
    • (2006) Exp. Oncol. , vol.28 , pp. 16-24
    • Malki, A.M.1    Gentry, J.2    Evans, S.C.3
  • 4
    • 67650337822 scopus 로고    scopus 로고
    • Two distinct pathways for metabolism of theophylline and caffeine are coexpressed in Pseudomonas putida CBB5
    • Yu CL, Louie TM, Summers R, Kale Y, Gopishetty S, Subramanian M. 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    Louie, T.M.2    Summers, R.3    Kale, Y.4    Gopishetty, S.5    Subramanian, M.6
  • 5
    • 79951486835 scopus 로고    scopus 로고
    • Characterization of a broad-specificity non-haem iron N-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 iron N-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
  • 6
    • 84861211147 scopus 로고    scopus 로고
    • Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids
    • Summers RM, Louie TM, Yu C-L, Gakhar L, Louie KC, Subramanian M. 2012. Novel, highly specific N-demethylases enable bacteria to live on caffeine and related purine alkaloids. J. Bacteriol. 194:2041-2049.
    • (2012) J. Bacteriol. , vol.194 , pp. 2041-2049
    • Summers, R.M.1    Louie, T.M.2    Yu, C.-L.3    Gakhar, L.4    Louie, K.C.5    Subramanian, M.6
  • 7
    • 0030796260 scopus 로고    scopus 로고
    • Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization
    • Link AJ, Phillips D, Church GM. 1997. Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization. J. Bacteriol. 179:6228-6237.
    • (1997) J. Bacteriol. , vol.179 , pp. 6228-6237
    • Link, A.J.1    Phillips, D.2    Church, G.M.3
  • 8
    • 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
  • 10
    • 0000122573 scopus 로고
    • PHYLIP-phylogeny inference package (version 3.2)
    • Felsenstein J. 1989. PHYLIP-phylogeny inference package (version 3.2). Cladistics 5:164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 12
    • 4944228604 scopus 로고    scopus 로고
    • Global transcriptional effects of a suppressor tRNA and the inactivation of the regulator frmR
    • Herring CD, Blattner FR. 2004. Global transcriptional effects of a suppressor tRNA and the inactivation of the regulator frmR. J. Bacteriol. 186:6714-6720.
    • (2004) J. Bacteriol. , vol.186 , pp. 6714-6720
    • Herring, C.D.1    Blattner, F.R.2
  • 13
    • 0026743341 scopus 로고
    • The electron-transport proteins of hydroxylating bacterial dioxygenases
    • Mason JR, Cammack R. 1992. The electron-transport proteins of hydroxylating bacterial dioxygenases. Annu. Rev. Microbiol. 46:277-305.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 277-305
    • Mason, J.R.1    Cammack, R.2
  • 14
    • 72749095187 scopus 로고    scopus 로고
    • Glutathione transferases are structural and functional outliers in the thioredoxin fold
    • Atkinson HJ, Babbitt PC. 2009. Glutathione transferases are structural and functional outliers in the thioredoxin fold. Biochemistry 48:11108-11116.
    • (2009) Biochemistry , vol.48 , pp. 11108-11116
    • Atkinson, H.J.1    Babbitt, P.C.2
  • 15
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: implications for classification of nonmammalian members of an ancient enzyme superfamily
    • Sheehan D, Meade G, Foley VM, Dowd CA. 2001. Structure, function and evolution of glutathione transferases: implications for classification of nonmammalian members of an ancient enzyme superfamily. Biochem. J. 360:1.
    • (2001) Biochem. J. , vol.360 , pp. 1
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 16
    • 0031056720 scopus 로고    scopus 로고
    • Bacterial glutathione S-transferases: what are they good for? J
    • Vuilleumier S. 1997. Bacterial glutathione S-transferases: what are they good for? J. Bacteriol. 179:1431-1441.
    • (1997) Bacteriol. , vol.179 , pp. 1431-1441
    • Vuilleumier, S.1
  • 17
    • 0027412924 scopus 로고
    • Metabolism and functions of glutathione in microorganisms
    • Penninckx MJ, Elskens MT. 1993. Metabolism and functions of glutathione in microorganisms. Adv. Microb. Physiol. 34:239-301.
    • (1993) Adv. Microb. Physiol. , vol.34 , pp. 239-301
    • Penninckx, M.J.1    Elskens, M.T.2
  • 18
    • 0028568602 scopus 로고
    • Eukaryotic translation elongation factor 1γ contains a glutathione transferase domain-study of a diverse, ancient protein super family using motif search and structural modeling
    • Koonin EV, Tatusov RL, Altschul SF, Bryant SH, Mushegian AR, Bork P, Valencia A. 1994. Eukaryotic translation elongation factor 1γ contains a glutathione transferase domain-study of a diverse, ancient protein super family using motif search and structural modeling. Protein Sci. 3:2045-2055.
    • (1994) Protein Sci. , vol.3 , pp. 2045-2055
    • Koonin, E.V.1    Tatusov, R.L.2    Altschul, S.F.3    Bryant, S.H.4    Mushegian, A.R.5    Bork, P.6    Valencia, A.7
  • 19
    • 0035793617 scopus 로고    scopus 로고
    • The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator
    • Dulhunty A, Gage P, Curtis S, Chelvanayagam G, Board P. 2001. The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator. J. Biol. Chem. 276:3319-3323.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3319-3323
    • Dulhunty, A.1    Gage, P.2    Curtis, S.3    Chelvanayagam, G.4    Board, P.5
  • 22
    • 0036158688 scopus 로고    scopus 로고
    • The elusive roles of bacterial glutathione S-transferases: new lessons from genomes
    • Vuilleumier S, Pagni M. 2002. The elusive roles of bacterial glutathione S-transferases: new lessons from genomes. Appl. Microbiol. Biotechnol. 58:138-146.
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 138-146
    • Vuilleumier, S.1    Pagni, M.2
  • 24
    • 0035167509 scopus 로고    scopus 로고
    • nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism
    • Zhou N-Y, Fuenmayor SL, Williams PA. 2001. nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism. J. Bacteriol. 183:700-708.
    • (2001) J. Bacteriol. , vol.183 , pp. 700-708
    • Zhou, N.-Y.1    Fuenmayor, S.L.2    Williams, P.A.3
  • 25
    • 0038455693 scopus 로고    scopus 로고
    • Implication of two glutathione S-transferases in the optimal metabolism of m-toluate by Sphingomonas yanoikuyae B1
    • Bae M, Sul W, Koh S-C, Lee J, Zylstra G, Kim Y, Kim E. 2003. Implication of two glutathione S-transferases in the optimal metabolism of m-toluate by Sphingomonas yanoikuyae B1. Antonie Van Leeuwenhoek 84:25-30.
    • (2003) Antonie Van Leeuwenhoek , vol.84 , pp. 25-30
    • Bae, M.1    Sul, W.2    Koh, S.-C.3    Lee, J.4    Zylstra, G.5    Kim, Y.6    Kim, E.7
  • 26
    • 0030789487 scopus 로고    scopus 로고
    • Molecular characterization of Fdx1, a putidaredoxin-type [2Fe-2S] ferredoxin able to transfer electrons to the dioxin dioxygenase of Sphingomonas sp
    • Armengaud J, Timmis KN. 1997. Molecular characterization of Fdx1, a putidaredoxin-type [2Fe-2S] ferredoxin able to transfer electrons to the dioxin dioxygenase of Sphingomonas sp. RW1. Eur. J. Biochem. 247:833-842.
    • (1997) RW1. Eur. J. Biochem. , vol.247 , pp. 833-842
    • Armengaud, J.1    Timmis, K.N.2
  • 27
    • 8744268521 scopus 로고    scopus 로고
    • Identification and functional analysis of two aromatic-ringhydroxylating dioxygenases from a sphingomonas strain that degrades various polycyclic aromatic hydrocarbons
    • Demanèche S, Meyer C, Micoud J, Louwagie M, Willison JC, Jouanneau Y. 2004. Identification and functional analysis of two aromatic-ringhydroxylating dioxygenases from a sphingomonas strain that degrades various polycyclic aromatic hydrocarbons. Appl. Environ. Microbiol. 70:6714-6725.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 6714-6725
    • Demanèche, S.1    Meyer, C.2    Micoud, J.3    Louwagie, M.4    Willison, J.C.5    Jouanneau, Y.6
  • 28
    • 0030790981 scopus 로고    scopus 로고
    • Glutathione S-transferase-encoding gene as a potential probe for environmental bacterial isolates capable of degrading polycyclic aromatic hydrocarbons
    • Lloyd-Jones G, Lau PC. 1997. Glutathione S-transferase-encoding gene as a potential probe for environmental bacterial isolates capable of degrading polycyclic aromatic hydrocarbons. Appl. Environ. Microbiol. 63:3286-3290.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3286-3290
    • Lloyd-Jones, G.1    Lau, P.C.2
  • 30
    • 0030029328 scopus 로고    scopus 로고
    • Degradation of caffeine and related methylxanthines by Serratia marcescens isolated from soil under coffee cultivation
    • Mazzafera P, Olsson O, Sandberg G. 1996. Degradation of caffeine and related methylxanthines by Serratia marcescens isolated from soil under coffee cultivation. Microb. Ecol. 31:199-207.
    • (1996) Microb. Ecol. , vol.31 , pp. 199-207
    • Mazzafera, P.1    Olsson, O.2    Sandberg, G.3
  • 31
    • 0032694011 scopus 로고    scopus 로고
    • Catabolism of caffeine and purification of a xanthine oxidade responsible for methyluric acids production in Pseudomonas putida L
    • Yamaoka-Yano DM, Mazzafera P. 1999. Catabolism of caffeine and purification of a xanthine oxidade responsible for methyluric acids production in Pseudomonas putida L. Braz. J. Microbiol. 30:62-70.
    • (1999) Braz. J. Microbiol. , vol.30 , pp. 62-70
    • Yamaoka-Yano, D.M.1    Mazzafera, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.