메뉴 건너뛰기




Volumn 27, Issue 3, 1998, Pages 563-571

The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K+ efflux system in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

LACTOYLGLUTATHIONE LYASE;

EID: 0031963196     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00701.x     Document Type: Article
Times cited : (111)

References (31)
  • 1
    • 0016139741 scopus 로고
    • Accumulation of toxic concentrations of methylglyoxal by wild-type Escherichia coli K12
    • Ackerman, R.S., Cozzarelli, N.R., and Epstein, W. (1974) Accumulation of toxic concentrations of methylglyoxal by wild-type Escherichia coli K12. J Bacteriol 119: 357-362.
    • (1974) J Bacteriol , vol.119 , pp. 357-362
    • Ackerman, R.S.1    Cozzarelli, N.R.2    Epstein, W.3
  • 4
    • 0001371953 scopus 로고
    • The mechanism of the glyoxalase I reaction, and the effect of ophthalmic acid as an inhibitor
    • Cliffe, E.E., and Waley, S.G. (1961) The mechanism of the glyoxalase I reaction, and the effect of ophthalmic acid as an inhibitor. Biochem J 79: 475-482.
    • (1961) Biochem J , vol.79 , pp. 475-482
    • Cliffe, E.E.1    Waley, S.G.2
  • 5
    • 0031579459 scopus 로고    scopus 로고
    • Isolation and sequencing of a gene coding for glyoxalase I activity from Salmonella tymphimurium and comparison with other glyoxylase I sequences
    • Clugston, S.L., Daub, E., Kinach, R., Miedema, D., Barnard, J.F.J., and Honek, J.F. (1997) Isolation and sequencing of a gene coding for glyoxalase I activity from Salmonella tymphimurium and comparison with other glyoxylase I sequences. Gene 186: 103-111.
    • (1997) Gene , vol.186 , pp. 103-111
    • Clugston, S.L.1    Daub, E.2    Kinach, R.3    Miedema, D.4    Barnard, J.F.J.5    Honek, J.F.6
  • 6
    • 0000544768 scopus 로고
    • The formation and catabolism of methylglyoxal during glycolysis in Escherichia coli
    • Cooper, R.A., and Anderson, A. (1970) The formation and catabolism of methylglyoxal during glycolysis in Escherichia coli. FEBS Lett 11: 273-276.
    • (1970) FEBS Lett , vol.11 , pp. 273-276
    • Cooper, R.A.1    Anderson, A.2
  • 8
  • 9
    • 0015155178 scopus 로고
    • Potassium transport in Escherichia coli K-12
    • Epstein, W., and Kim, B.S. (1971) Potassium transport in Escherichia coli K-12. J Bacteriol 108: 639-644.
    • (1971) J Bacteriol , vol.108 , pp. 639-644
    • Epstein, W.1    Kim, B.S.2
  • 10
    • 0027491161 scopus 로고
    • Activation of potassium channels during metabolite detoxification in Escherichia coli
    • Ferguson, G.P., Munro, A.W., Douglas, R.M., McLaggan, D., and Booth, I.R. (1993) Activation of potassium channels during metabolite detoxification in Escherichia coli. Mol Microbiol 9: 1-7.
    • (1993) Mol Microbiol , vol.9 , pp. 1-7
    • Ferguson, G.P.1    Munro, A.W.2    Douglas, R.M.3    McLaggan, D.4    Booth, I.R.5
  • 11
    • 0028786475 scopus 로고
    • Potassium channel activation by glutathione-S-conjugates in Escherichia coli: Protection against methylglyoxal is mediated by cytoplasmic acidification
    • Ferguson, G.P., McLaggan, D., and Booth, I.R. (1995) Potassium channel activation by glutathione-S-conjugates in Escherichia coli: protection against methylglyoxal is mediated by cytoplasmic acidification. Mol Microbiol 17: 1025-1033.
    • (1995) Mol Microbiol , vol.17 , pp. 1025-1033
    • Ferguson, G.P.1    McLaggan, D.2    Booth, I.R.3
  • 12
    • 0029884672 scopus 로고    scopus 로고
    • + uptake system Kdp sensitises cells of Escherichia coli to methylglyoxal
    • + uptake system Kdp sensitises cells of Escherichia coli to methylglyoxal. J Bacteriol 178: 3957-3961.
    • (1996) J Bacteriol , vol.178 , pp. 3957-3961
    • Ferguson, G.P.1    Chacko, A.D.2    Lee, C.3    Booth, I.R.4
  • 13
    • 0031049947 scopus 로고    scopus 로고
    • Survival during exposure to the electrophile reagent N-ethylmaleimide in Escherichia coli: Role of KefB and KefC potassium channels
    • Ferguson, G.P., Nikolaev, Y., McLaggan, D., MacLean, M., and Booth, I.R. (1997) Survival during exposure to the electrophile reagent N-ethylmaleimide in Escherichia coli: role of KefB and KefC potassium channels. J Bacteriol 179: 1007-1012.
    • (1997) J Bacteriol , vol.179 , pp. 1007-1012
    • Ferguson, G.P.1    Nikolaev, Y.2    McLaggan, D.3    MacLean, M.4    Booth, I.R.5
  • 14
    • 0015130565 scopus 로고
    • Lethal synthesis of methylglyoxal by Escherichia coli during unregulated glycerol metabolism
    • Freedberg, W.B., Kistler, W.S., and Lin, E.C.C. (1971) Lethal synthesis of methylglyoxal by Escherichia coli during unregulated glycerol metabolism. J Bacteriol 108: 137-144.
    • (1971) J Bacteriol , vol.108 , pp. 137-144
    • Freedberg, W.B.1    Kistler, W.S.2    Lin, E.C.C.3
  • 15
    • 0001515246 scopus 로고
    • The regulation of Escherichia coli methylglyoxal synthase: A new control site in glycolysis?
    • Hopper, D.J., and Cooper, R.A. (1971) The regulation of Escherichia coli methylglyoxal synthase: a new control site in glycolysis? FEBS Lett 13: 213-216.
    • (1971) FEBS Lett , vol.13 , pp. 213-216
    • Hopper, D.J.1    Cooper, R.A.2
  • 16
    • 0027281387 scopus 로고
    • Human glyoxalase I: cDNA, cloning, expression and sequence similarity to glyoxalase I from Pseudomonas putida
    • Kim, N-S., Umezawa, Y., Ohmura, S., and Kato, S. (1993) Human glyoxalase I: cDNA, cloning, expression and sequence similarity to glyoxalase I from Pseudomonas putida. J Biol Chem 268: 11217-11221.
    • (1993) J Biol Chem , vol.268 , pp. 11217-11221
    • Kim, N.-S.1    Umezawa, Y.2    Ohmura, S.3    Kato, S.4
  • 17
    • 0023669069 scopus 로고
    • The physical map of the whole Escherichia coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., Akiyama, K., and Isono, K. (1987) The physical map of the whole Escherichia coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50: 495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 18
    • 0015040186 scopus 로고
    • Genetic recombination in Escherichia coli: The role of exonuclease 1
    • Kushner, S.R., Nagaishi, H., Templin, A., and Clark, A.J. (1971) Genetic recombination in Escherichia coli: the role of exonuclease 1. Proc Natl Acad Sci USA 68: 824-827.
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 824-827
    • Kushner, S.R.1    Nagaishi, H.2    Templin, A.3    Clark, A.J.4
  • 19
    • 0027973979 scopus 로고
    • The gene encoding glyoxalase I from Pseudomonas putida: Cloning, over-expression and sequence comparisons with human glyoxalase I
    • Lu, T., Creighton, D.J., Antoine, M., Fenselau, C., and Lovett, P.S. (1994) The gene encoding glyoxalase I from Pseudomonas putida: cloning, over-expression and sequence comparisons with human glyoxalase I. Gene 150: 93-96.
    • (1994) Gene , vol.150 , pp. 93-96
    • Lu, T.1    Creighton, D.J.2    Antoine, M.3    Fenselau, C.4    Lovett, P.S.5
  • 20
    • 0028939260 scopus 로고
    • Glyoxalase III from Escherichia coli: A single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione
    • Misra, K., Banerjee, A.B., Ray, S., and Ray, M. (1995) Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione. Biochem J 305: 999-1003.
    • (1995) Biochem J , vol.305 , pp. 999-1003
    • Misra, K.1    Banerjee, A.B.2    Ray, S.3    Ray, M.4
  • 21
    • 0029872670 scopus 로고    scopus 로고
    • Reduction of methylglyoxal in Escherichia coli K12 by an aldehyde reductase and alcohol dehydrogenase
    • Misra, K., Banerjee, A.B., Ray, S., and Ray, M. (1996) Reduction of methylglyoxal in Escherichia coli K12 by an aldehyde reductase and alcohol dehydrogenase. Mol Cell Biochem 156: 117-124.
    • (1996) Mol Cell Biochem , vol.156 , pp. 117-124
    • Misra, K.1    Banerjee, A.B.2    Ray, S.3    Ray, M.4
  • 22
    • 0026036336 scopus 로고
    • The cloning and sequence of the gene for the glutathione-regulated potassium efflux system KefC of Escherichia coli
    • Munro, A.W., Ritchie, G.Y., Lamb, A.J., Douglas, R.M., and Booth, I.R. (1991) The cloning and sequence of the gene for the glutathione-regulated potassium efflux system KefC of Escherichia coli. Mol Microbiol 5: 607-616.
    • (1991) Mol Microbiol , vol.5 , pp. 607-616
    • Munro, A.W.1    Ritchie, G.Y.2    Lamb, A.J.3    Douglas, R.M.4    Booth, I.R.5
  • 23
    • 0242504773 scopus 로고
    • Metabolism of a-ketoaldehydes in yeasts: Purification and characterization of glyoxalase II from Saccharomyces cerevisiae
    • Murata, K., Inoue, Y., Watanabi, K., Fukuda, Y., Saikusa, T., Shimosaka, M., et al. (1986) Metabolism of a-ketoaldehydes in yeasts: purification and characterization of glyoxalase II from Saccharomyces cerevisiae. Agric Biol Chem 50: 135-142.
    • (1986) Agric Biol Chem , vol.50 , pp. 135-142
    • Murata, K.1    Inoue, Y.2    Watanabi, K.3    Fukuda, Y.4    Saikusa, T.5    Shimosaka, M.6
  • 25
    • 0345096392 scopus 로고
    • Spectrophotometric enzymatic methods for the determination of aldehydes and ketoaldehydes
    • Racker, E. (1951) Spectrophotometric enzymatic methods for the determination of aldehydes and ketoaldehydes. Methods Enzymol 3: 293-296.
    • (1951) Methods Enzymol , vol.3 , pp. 293-296
    • Racker, E.1
  • 26
    • 0021756302 scopus 로고
    • Genetic studies on the phs locus of Escherichia coli, a mutation causing pleiotropic lesions in metabolism and pH homeostasis
    • Rowland, G.G., Giffard, P.M., and Booth, I.R. (1984) Genetic studies on the phs locus of Escherichia coli, a mutation causing pleiotropic lesions in metabolism and pH homeostasis. FEBS Lett 173: 295-300.
    • (1984) FEBS Lett , vol.173 , pp. 295-300
    • Rowland, G.G.1    Giffard, P.M.2    Booth, I.R.3
  • 28
    • 0030977195 scopus 로고    scopus 로고
    • Diffusion-dependent kinetic properties of glyoxalase I and estimates of the steady state concentrations of glyoxalase-pathway intermediates in glycolyzing erythrocytes
    • Shin, M.J., Edinger, J.W., and Creighton, D.J. (1997) Diffusion-dependent kinetic properties of glyoxalase I and estimates of the steady state concentrations of glyoxalase-pathway intermediates in glycolyzing erythrocytes. Eur J Biochem 244: 852-857.
    • (1997) Eur J Biochem , vol.244 , pp. 852-857
    • Shin, M.J.1    Edinger, J.W.2    Creighton, D.J.3
  • 29
    • 0022719327 scopus 로고
    • pHG165: A pBR322 copy number derivative of pUC8 for cloning and expression
    • Stewart, G.S.A.B., Lubinsky-Mink, S., Jackson, C.G., Cassel, A., and Kuhn, J. (1986) pHG165: a pBR322 copy number derivative of pUC8 for cloning and expression. Plasmid 18: 172-181.
    • (1986) Plasmid , vol.18 , pp. 172-181
    • Stewart, G.S.A.B.1    Lubinsky-Mink, S.2    Jackson, C.G.3    Cassel, A.4    Kuhn, J.5
  • 30
    • 0031983922 scopus 로고    scopus 로고
    • From famine to feast: The role of methylglyoxal production in Escherichia coli
    • Tötemeyer, S., Booth, N.A., Nichols, W.W., Dunbar, B., and Booth, I.R. (1998) From famine to feast: the role of methylglyoxal production in Escherichia coli. Mol Microbiol 27: 553-562.
    • (1998) Mol Microbiol , vol.27 , pp. 553-562
    • Tötemeyer, S.1    Booth, N.A.2    Nichols, W.W.3    Dunbar, B.4    Booth, I.R.5
  • 31
    • 0015791813 scopus 로고
    • Purification and characterization of S-2-hydroxyacylglutathione hydrolase glyoxalase II from human liver
    • Uotila, L. (1973) Purification and characterization of S-2-hydroxyacylglutathione hydrolase glyoxalase II from human liver. Biochemistry 12: 3944-3951.
    • (1973) Biochemistry , vol.12 , pp. 3944-3951
    • Uotila, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.