메뉴 건너뛰기




Volumn 94, Issue 3, 2012, Pages 588-596

Distribution of glutathione transferases in Gram-positive bacteria and Archaea

Author keywords

Archaea; Bacterial glutathione transferase; Glutathione; Gram positive bacteria; In silico analysis

Indexed keywords

BACTERIAL ENZYME; FOSFOMYCIN; FUNGAL PROTEIN; GLUTATHIONE TRANSFERASE; UNCLASSIFIED DRUG; URE2 PROTEIN;

EID: 84857048168     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2011.09.008     Document Type: Short Survey
Times cited : (40)

References (45)
  • 2
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily
    • DOI 10.1042/0264-6021:3600001
    • D. Sheehan, G. Meade, V.M. Foley, and C.A. Dowd Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily Biochem. J. 360 2001 1 16 (Pubitemid 33081943)
    • (2001) Biochemical Journal , vol.360 , Issue.1 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 3
    • 79954572279 scopus 로고    scopus 로고
    • Glutathione transferases: A structural perspective
    • A. Oakley Glutathione transferases: a structural perspective Drug Metabol. Rev. 43 2011 138 151
    • (2011) Drug Metabol. Rev. , vol.43 , pp. 138-151
    • Oakley, A.1
  • 5
    • 0036158688 scopus 로고    scopus 로고
    • The elusive roles of bacterial glutathione S-transferases: New lessons from genomes
    • DOI 10.1007/s00253-001-0836-0
    • S. Vuilleumier, and M. Pagni The elusive roles of bacterial glutathione S-transferases: new lessons from genomes Appl. Microbiol. Biotechnol. 58 2002 138 146 (Pubitemid 34118986)
    • (2002) Applied Microbiology and Biotechnology , vol.58 , Issue.2 , pp. 138-146
    • Vuilleumier, S.1    Pagni, M.2
  • 6
  • 8
    • 0028952595 scopus 로고
    • Glutathione-S-transferase activity and metabolism of glutathione conjugates by Rhizosphere bacteria
    • R.M. Zablotowicz, R.E. Hoagland, M.A. Locke, and W.J. Hickey Glutathione-S-transferase activity and metabolism of glutathione conjugates by Rhizosphere bacteria Appl. Environ. Microbiol. 61 1995 1054 1060
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1054-1060
    • Zablotowicz, R.M.1    Hoagland, R.E.2    Locke, M.A.3    Hickey, W.J.4
  • 9
    • 0034020589 scopus 로고    scopus 로고
    • Characterization of the gene cluster involved in isoprene metabolism in Rhodococcus sp. strain AD45
    • DOI 10.1128/JB.182.7.1956-1963.2000
    • J.E.T. van Hylckama Vlieg, H. Leemhuis, J.H. Lutje Spelberg, and D.B. Janssen Characterization of the gene cluster involved in isoprene metabolism in Rhodococcus sp. strain AD45 J. Bacteriol. 182 2000 1956 1963 (Pubitemid 30165385)
    • (2000) Journal of Bacteriology , vol.182 , Issue.7 , pp. 1956-1963
    • Van Hylckama Vlieg, J.E.T.1    Leemhuis, H.2    Lutje Spelberg, J.H.3    Janssen, D.B.4
  • 10
    • 0037229210 scopus 로고    scopus 로고
    • Glutathione S-transferase isoenzymes from Streptomyces griseus
    • DOI 10.1128/AEM.69.1.707-710.2003
    • K. Dhar, A. Dhar, and J.P. Rosazza Glutathione S-transferase isoenzymes from Streptomyces griseus Appl. Environ. Microbiol. 69 2003 707 710 (Pubitemid 36077546)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.1 , pp. 707-710
    • Dhar, K.1    Dhar, A.2    Rosazza, J.P.N.3
  • 11
    • 77951857786 scopus 로고    scopus 로고
    • Preliminary analysis of glutathione S-transferase homolog from Lactobacillus casei Zhang
    • W.Y. Zhang, D.L. Yu, Z.H. Sun, C. Airideng, S.N. Hu, H. Meng, and H.P. Zhang Preliminary analysis of glutathione S-transferase homolog from Lactobacillus casei Zhang Ann. Microbiol. 59 2009 727 731
    • (2009) Ann. Microbiol. , vol.59 , pp. 727-731
    • Zhang, W.Y.1    Yu, D.L.2    Sun, Z.H.3    Airideng, C.4    Hu, S.N.5    Meng, H.6    Zhang, H.P.7
  • 12
    • 0019741605 scopus 로고
    • Assay for differentiation of glutathione S-transferases
    • W.H. Habig, and W.B. Jakoby Assay for differentiation of glutathione S-transferases Methods Enzymol. 77 1981 398 405
    • (1981) Methods Enzymol. , vol.77 , pp. 398-405
    • Habig, W.H.1    Jakoby, W.B.2
  • 15
    • 18944397128 scopus 로고    scopus 로고
    • A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis
    • DOI 10.1128/JB.187.11.3839-3847.2005
    • S. Gopal, I. Borovok, A. Ofer, M. Yanku, G. Cohen, W. Goebel, J. Kreft, and Y. Aharonowitz A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis J. Bacteriol. 187 2005 3839 3847 (Pubitemid 40705589)
    • (2005) Journal of Bacteriology , vol.187 , Issue.11 , pp. 3839-3847
    • Gopal, S.1    Borovok, I.2    Ofer, A.3    Yanku, M.4    Cohen, G.5    Goebel, W.6    Kreft, J.7    Aharonowitz, Y.8
  • 16
    • 15744398210 scopus 로고    scopus 로고
    • Glutathione synthesis in Streptococcus agalactiae: One protein accounts for γ-glutamylcysteine synthetase and glutathione synthetase activities
    • DOI 10.1074/jbc.M414326200
    • B.E. Janowiak, and O.W. Griffith Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities J. Biol. Chem. 280 2005 11829 11839 (Pubitemid 40418497)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11829-11839
    • Janowiak, B.E.1    Griffith, O.W.2
  • 18
    • 77951537330 scopus 로고    scopus 로고
    • Glutathione protects Lactobacillus sanfranciscensis against freeze-thawing, freeze-drying, and cold treatment
    • J. Zhang, G.C. Du, Y. Zhang, X.Y. Liao, M. Wang, Y. Li, and J. Chen Glutathione protects Lactobacillus sanfranciscensis against freeze-thawing, freeze-drying, and cold treatment Appl. Environ. Microbiol. 76 2010 2989 2996
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 2989-2996
    • Zhang, J.1    Du, G.C.2    Zhang, Y.3    Liao, X.Y.4    Wang, M.5    Li, Y.6    Chen, J.7
  • 20
    • 27444432343 scopus 로고    scopus 로고
    • Determination of coenzyme A levels in Pyrococcus furiosus and other Archaea: Implications for a general role for coenzyme A in thermophiles
    • DOI 10.1016/j.femsle.2005.09.004, PII S0378109705006178
    • C.S. Hummel, K.M. Lancaster, and E.J. Crane 3rd Determination of coenzyme A levels in Pyrococcus furiosus and other Archaea: implications for a general role for coenzyme A in thermophiles FEMS Microbiol. Lett. 252 2005 229 234 (Pubitemid 41531648)
    • (2005) FEMS Microbiology Letters , vol.252 , Issue.2 , pp. 229-234
    • Hummel, C.S.1    Lancaster, K.M.2    Crane III, E.J.3
  • 21
    • 0022183623 scopus 로고
    • Gamma-glutamylcysteine: A substrate for glutathione S-transferases
    • DOI 10.1016/0006-2952(85)90224-2
    • M. Sugimoto, J. Kuhlenkamp, M. Ookhtens, T.Y. Aw, J. Reeve Jr., and N. Kaplowitz Gamma-glutamylcysteine: a substrate for glutathione S-transferases Biochem. Pharmacol. 34 1985 3643 3647 (Pubitemid 16251345)
    • (1985) Biochemical Pharmacology , vol.34 , Issue.20 , pp. 3643-3647
    • Sugimoto, M.1    Kuhlenkamp, J.2    Ookhtens, M.3
  • 23
    • 0032526942 scopus 로고    scopus 로고
    • A mixed disulfide bond in bacterial glutathione transferase: Functional and evolutionary implications
    • J. Rossjohn, G. Polekhina, S.C. Feil, N. Allocati, M. Masulli, C. Di Ilio, and M.W. Parker A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications Structure 15 1998 721 734 (Pubitemid 28301206)
    • (1998) Structure , vol.6 , Issue.6 , pp. 721-734
    • Rossjohn, J.1    Polekhina, G.2    Feil, S.C.3    Allocati, N.4    Masulli, M.5    Di Iiio, C.6    Parker, M.W.7
  • 25
    • 33750044065 scopus 로고    scopus 로고
    • Structures of ternary complexes of BphK, a bacterial glutathione S-transferase that reductively dechlorinates polychlorinated biphenyl metabolites
    • DOI 10.1074/jbc.M603125200
    • E.I. Tocheva, P.D. Fortin, L.D. Eltis, and M.E.P. Murphy Structures of ternary complexes of BphK, a bacterial glutathione S-transferase that reductively dechlorinates polychlorinated biphenyl metabolites J. Biol. Chem. 281 2006 30933 30940 (Pubitemid 44582148)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.41 , pp. 30933-30940
    • Tocheva, E.I.1    Fortin, P.D.2    Eltis, L.D.3    Murphy, M.E.P.4
  • 26
    • 40549133470 scopus 로고    scopus 로고
    • Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site
    • DOI 10.1002/prot.21835
    • N. Allocati, L. Federici, M. Masulli, B. Favaloro, and C. Di Ilio Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site Proteins 71 2008 16 23 (Pubitemid 351358587)
    • (2008) Proteins: Structure, Function and Genetics , vol.71 , Issue.1 , pp. 16-23
    • Allocati, N.1    Federici, L.2    Masulli, M.3    Favaloro, B.4    Di Ilio, C.5
  • 27
    • 77956029069 scopus 로고    scopus 로고
    • Characterization of the hydrophobic substrate-binding site of the bacterial Beta class glutathione transferase from Proteus mirabilis
    • L. Federici, M. Masulli, C. Di Ilio, and N. Allocati Characterization of the hydrophobic substrate-binding site of the bacterial Beta class glutathione transferase from Proteus mirabilis Prot. Eng. Des. Sel. 23 2010 743 750
    • (2010) Prot. Eng. Des. Sel. , vol.23 , pp. 743-750
    • Federici, L.1    Masulli, M.2    Di Ilio, C.3    Allocati, N.4
  • 28
    • 32944467164 scopus 로고    scopus 로고
    • Evolutionary conserved structural motifs in bacterial GST (glutathione S-transferase) are involved in protein folding and stability
    • DOI 10.1042/BJ20051367
    • N. Allocati, M. Masulli, M. Pietracupa, L. Federici, and C. Di Ilio Evolutionarily conserved structural motifs in bacterial glutathione transferase are involved in protein folding and stability Biochem. J. 394 2006 11 17 (Pubitemid 43259650)
    • (2006) Biochemical Journal , vol.394 , Issue.1 , pp. 11-17
    • Allocati, N.1    Masulli, M.2    Pietracupa, M.3    Federici, L.4    Di Ilio, C.5
  • 29
    • 0035943609 scopus 로고    scopus 로고
    • The folding and stability of human alpha class glutathione transferase A1-1 depend on distinct roles of a conserved N-capping box and hydrophobic staple motif
    • R. Cocco, G. Stenberg, B. Dragani, D. Rossi Principe, D. Paludi, B. Mannervik, and A. Aceto The folding and stability of human alpha class glutathione transferase A1-1 depend on distinct roles of a conserved N-capping box and hydrophobic staple motif J. Biol. Chem. 276 2001 32177 32183
    • (2001) J. Biol. Chem. , vol.276 , pp. 32177-32183
    • Cocco, R.1    Stenberg, G.2    Dragani, B.3    Rossi Principe, D.4    Paludi, D.5    Mannervik, B.6    Aceto, A.7
  • 30
    • 64049098665 scopus 로고    scopus 로고
    • A conserved hydrogen-bond network stabilizes the structure of beta class glutathione S-transferases
    • L. Federici, M. Masulli, S. Gianni, C. Di Ilio, and N. Allocati A conserved hydrogen-bond network stabilizes the structure of beta class glutathione S-transferases Biochem. Biophys. Res. Commun. 382 2009 525 529
    • (2009) Biochem. Biophys. Res. Commun. , vol.382 , pp. 525-529
    • Federici, L.1    Masulli, M.2    Gianni, S.3    Di Ilio, C.4    Allocati, N.5
  • 31
    • 64549108884 scopus 로고    scopus 로고
    • Evolution of the antibiotic resistance protein, FosA, is linked to a catalytically promiscuous progenitor
    • D.W. Brown, M.R. Schaab, W.R. Birmingham, and R.N. Armstrong Evolution of the antibiotic resistance protein, FosA, is linked to a catalytically promiscuous progenitor Biochemistry 48 2009 1847 1849
    • (2009) Biochemistry , vol.48 , pp. 1847-1849
    • Brown, D.W.1    Schaab, M.R.2    Birmingham, W.R.3    Armstrong, R.N.4
  • 32
    • 24044523194 scopus 로고    scopus 로고
    • Functional analysis of active site residues of the fosfomycin resistance enzyme FosA from Pseudomonas aeruginosa
    • DOI 10.1074/jbc.M501052200
    • Z. Beharry, and T. Palzkill Functional analysis of active site residues of the fosfomycin resistance enzyme FosA from Pseudomonas aeruginosa J. Biol. Chem. 280 2005 17786 17791 (Pubitemid 41389017)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 17786-17791
    • Beharry, Z.1    Palzkill, T.2
  • 33
    • 33748347924 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases
    • DOI 10.1042/BJ20060034
    • A. Garcerá, L. Barreto, L. Piedrafita, J. Tamarit, and E. Herrero Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases Biochem. J. 398 2006 187 196 (Pubitemid 44338475)
    • (2006) Biochemical Journal , vol.398 , Issue.2 , pp. 187-196
    • Garcera, A.1    Barreto, L.2    Piedrafita, L.3    Tamarit, J.4    Herrero, E.5
  • 34
    • 77954947303 scopus 로고    scopus 로고
    • S-glutathionyl-(chloro)hydroquinone reductases: A novel class of glutathione transferases
    • L. Xun, S.M. Belchik, R. Xun, Y. Huang, H. Zhou, E. Sanchez, C. Kang, and P.G. Board S-glutathionyl-(chloro)hydroquinone reductases: a novel class of glutathione transferases Biochem. J. 428 2010 419 427
    • (2010) Biochem. J. , vol.428 , pp. 419-427
    • Xun, L.1    Belchik, S.M.2    Xun, R.3    Huang, Y.4    Zhou, H.5    Sanchez, E.6    Kang, C.7    Board, P.G.8
  • 36
    • 0035856522 scopus 로고    scopus 로고
    • Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds
    • DOI 10.1021/bi011007b
    • L. Bousset, H. Belrhali, R. Melki, and S. Morera Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds Biochemistry 40 2001 13564 13573 (Pubitemid 33130784)
    • (2001) Biochemistry , vol.40 , Issue.45 , pp. 13564-13573
    • Bousset, L.1    Belrhali, H.2    Melki, R.3    Morera, S.4
  • 37
    • 0035156642 scopus 로고    scopus 로고
    • Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae
    • DOI 10.1016/S0969-2126(00)00553-0, PII S0969212600005530
    • L. Bousset, H. Belrhali, J. Janin, R. Melki, and S. Morera Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae Structure 9 2001 39 46 (Pubitemid 32064348)
    • (2001) Structure , vol.9 , Issue.1 , pp. 39-46
    • Bousset, L.1    Belrhali, H.2    Janin, J.3    Melki, R.4    Morera, S.5
  • 38
    • 78649990743 scopus 로고    scopus 로고
    • Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural context
    • L. Bousset, J. Bonnefoy, Y. Sourigues, F. Wien, and R. Melki Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural context PLoS One 5 2010 e9760
    • (2010) PLoS One , vol.5 , pp. 9760
    • Bousset, L.1    Bonnefoy, J.2    Sourigues, Y.3    Wien, F.4    Melki, R.5
  • 39
    • 0028298404 scopus 로고
    • Starvation-induced expression of SspA and SspB: The effects of a null mutation in sspA on Escherichia coli protein synthesis and survival during growth and prolonged starvation
    • DOI 10.1111/j.1365-2958.1994.tb00381.x
    • M.D. Williams, T.X. Ouyang, and M.C. Flickinger Starvation-induced expression of SspA and SspB: the effects of a null mutation in sspA on Escherichia coli protein synthesis and survival during growth and prolonged starvation Mol. Microbiol. 11 1994 1029 1043 (Pubitemid 24201620)
    • (1994) Molecular Microbiology , vol.11 , Issue.6 , pp. 1029-1043
    • Williams, M.D.1    Ouyang, T.X.2    Flickinger, M.C.3
  • 40
    • 20444476586 scopus 로고    scopus 로고
    • Structural basis for the function of stringent starvation protein A as a transcription factor
    • DOI 10.1074/jbc.M501444200
    • A.M. Hansen, Y. Gu, M. Li, M. Andrykovitch, D.S. Waugh, D.J. Jin, and X. Ji Structural basis for the function of stringent starvation protein A as a transcription factor J. Biol. Chem. 280 2005 17380 17391 (Pubitemid 41389208)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17380-17391
    • Hansen, A.-M.1    Gu, Y.2    Li, M.3    Andrykovitch, M.4    Waugh, D.S.5    Jin, D.J.6    Ji, X.7
  • 41
    • 33746474688 scopus 로고    scopus 로고
    • Glutathione transferases in the genomics era: New insights and perspectives
    • DOI 10.1016/j.bioeng.2006.05.020, PII S1389034406000414
    • C. Frova Glutathione transferases in the genomics era: new insights and perspectives Biomol. Eng. 23 2006 149 169 (Pubitemid 44142335)
    • (2006) Biomolecular Engineering , vol.23 , Issue.4 , pp. 149-169
    • Frova, C.1
  • 42
    • 0033823160 scopus 로고    scopus 로고
    • The phylogeny of proteobacteria: Relationships to other eubacterial phyla and eukaryotes
    • R.S. Gupta The phylogeny of proteobacteria: relationships to other eubacterial phyla and eukaryotes FEMS Microbiol. Rev. 24 2000 367 402
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 367-402
    • Gupta, R.S.1
  • 43
    • 0037386619 scopus 로고    scopus 로고
    • Were Gram-positive rods the first bacteria?
    • DOI 10.1016/S0966-842X(03)00063-5
    • A.L. Koch Were Gram-positive rods the first bacteria? Trends Microbiol. 11 2003 166 170 (Pubitemid 36428830)
    • (2003) Trends in Microbiology , vol.11 , Issue.4 , pp. 166-170
    • Koch, A.L.1
  • 45
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • K. Tamura, J. Dudley, M. Nei, and S. Kumar MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0 Mol. Biol. Evol. 24 2007 1596 1599 (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.