메뉴 건너뛰기




Volumn 186, Issue 1, 1997, Pages 103-111

Isolation and sequencing of a gene coding for glyoxalase I activity from Salmonella typhimurium and comparison with other glyoxalase I sequences

Author keywords

Isomerase; S D lactoylglutathione methylglyoxal lyase; Zn2+ ligands

Indexed keywords

LACTOYLGLUTATHIONE LYASE; METHYLGLYOXAL; ZINC;

EID: 0031579459     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(96)00691-9     Document Type: Article
Times cited : (28)

References (39)
  • 1
    • 0022445668 scopus 로고
    • Inhibition of mammalian glyoxalase I (lactoylglutathione lyase) by N-acylated S-blocked glutathione derivatives as a probe for the role of the N-site of glutathione in glyoxalase I mechanism
    • Al-Timari, A. and Douglas, K.T. (1986) Inhibition of mammalian glyoxalase I (lactoylglutathione lyase) by N-acylated S-blocked glutathione derivatives as a probe for the role of the N-site of glutathione in glyoxalase I mechanism. Biochim. Biophys. Acta 870, 160-168.
    • (1986) Biochim. Biophys. Acta , vol.870 , pp. 160-168
    • Al-Timari, A.1    Douglas, K.T.2
  • 4
  • 6
    • 0022545386 scopus 로고
    • The glyoxalase enigma-the biological consequences of a ubiquitous enzyme
    • Carrington, S.J. and Douglas, K.T. (1986) The glyoxalase enigma-the biological consequences of a ubiquitous enzyme. IRCS Med. Sci. 14, 763-768.
    • (1986) IRCS Med. Sci. , vol.14 , pp. 763-768
    • Carrington, S.J.1    Douglas, K.T.2
  • 7
    • 0029610872 scopus 로고
    • Molecular characterization of glyoxalase-I from a higher plant; upregulation by stress
    • Espartero, J., Sánchez-Aguayo, I. and Pardo, J.M. (1995) Molecular characterization of glyoxalase-I from a higher plant; upregulation by stress. Plant Mol. Biol. 29, 1223-1233.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 1223-1233
    • Espartero, J.1    Sánchez-Aguayo, I.2    Pardo, J.M.3
  • 9
    • 0018198591 scopus 로고
    • Concanavalin A increases glyoxalase enzyme activities in polymorphonuclear leukocytes and lymphocytes
    • Gillespie, E. (1978) Concanavalin A increases glyoxalase enzyme activities in polymorphonuclear leukocytes and lymphocytes. J. Immunol. 121, 923-925.
    • (1978) J. Immunol. , vol.121 , pp. 923-925
    • Gillespie, E.1
  • 10
    • 0026465674 scopus 로고
    • Inhibition of glyoxalase I by the enediol mimic S-(N-hydroxy-N-methylcarbamoyl)glutathione: The possible basis of a tumor-selective anticancer strategy
    • Hamilton, D.S. and Creighton, D.J. (1992) Inhibition of glyoxalase I by the enediol mimic S-(N-hydroxy-N-methylcarbamoyl)glutathione: The possible basis of a tumor-selective anticancer strategy. J. Biol. Chem. 267, 24933-24936.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24933-24936
    • Hamilton, D.S.1    Creighton, D.J.2
  • 11
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading Pseudomonad
    • Han, S., Eltis, L.D., Timmis, K.N., Muchmore, S.W. and Bolin, J.T. (1995) Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading Pseudomonad. Science 270, 976-980.
    • (1995) Science , vol.270 , pp. 976-980
    • Han, S.1    Eltis, L.D.2    Timmis, K.N.3    Muchmore, S.W.4    Bolin, J.T.5
  • 12
    • 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
  • 13
    • 0024234855 scopus 로고
    • CLUSTAL: a package for performing multiple sequence alignment on a microcomputer
    • Higgins, D.G. and Sharp, P.M. (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73, 237-244.
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 14
    • 0019871880 scopus 로고
    • Concentration of activated intermediates of the fructose-1,6-bisphosphate aldolase and triosephosphate isomerase reactions
    • Iyengar, R. and Rose, I.A. (1981) Concentration of activated intermediates of the fructose-1,6-bisphosphate aldolase and triosephosphate isomerase reactions. Biochemistry 20, 1223-1229.
    • (1981) Biochemistry , vol.20 , pp. 1223-1229
    • Iyengar, R.1    Rose, I.A.2
  • 15
    • 0028330140 scopus 로고
    • Characterization of interactions and metal ion binding sites in proteins
    • Jernigan, R., Raghunathan, G. and Bahar, I. (1994) Characterization of interactions and metal ion binding sites in proteins. Curr. Opin. Struct. Biol. 4, 256-263.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 256-263
    • Jernigan, R.1    Raghunathan, G.2    Bahar, I.3
  • 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
    • 0029053976 scopus 로고
    • Evidence for a (triosephosphate isomerase-like) `catalytic loop' near the active site of glyoxalase I
    • Lan, Y., Lu, T., Lovett, P.S. and Creighton, D.J. (1995) Evidence for a (triosephosphate isomerase-like) `catalytic loop' near the active site of glyoxalase I. J. Biol. Chem. 270, 12957-12960.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12957-12960
    • Lan, Y.1    Lu, T.2    Lovett, P.S.3    Creighton, D.J.4
  • 18
    • 0027973979 scopus 로고
    • The gene encoding glyoxalase I from Pseudomonas putida: cloning, overexpression, 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, overexpression, 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
  • 19
    • 0028831526 scopus 로고
    • Aminoacetone metabolism by semicarbazide-sensitive amine oxidase in rat aorta
    • Lyles, G.A. and Chalmers, J. (1995) Aminoacetone metabolism by semicarbazide-sensitive amine oxidase in rat aorta. Biochem. Pharmacol. 49, 416-419.
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 416-419
    • Lyles, G.A.1    Chalmers, J.2
  • 21
    • 0023984847 scopus 로고
    • Optimal alignments in linear space
    • Myers, E.W. and Miller, W. (1988) Optimal alignments in linear space. Comput. Appl. Biosci. 4, 11-17.
    • (1988) Comput. Appl. Biosci. , vol.4 , pp. 11-17
    • Myers, E.W.1    Miller, W.2
  • 23
    • 0001084551 scopus 로고
    • Enzymatic conversion of α-keto aldehydes to optically active α-hydroxy acids using glyoxalase I and II
    • Patterson, M.A.K., Szajewski, R.P. and Whitesides, G.M. (1981) Enzymatic conversion of α-keto aldehydes to optically active α-hydroxy acids using glyoxalase I and II. J. Org. Chem. 46, 4682-4685.
    • (1981) J. Org. Chem. , vol.46 , pp. 4682-4685
    • Patterson, M.A.K.1    Szajewski, R.P.2    Whitesides, G.M.3
  • 24
    • 0021112010 scopus 로고
    • The glutathione-dependent glyoxalase pathway in the yeast Saccharomyces cerevisiae: a vital defense line against methylglyoxal produced during glycerol catabolism
    • Penninckx, M.J., Jaspers, C.J. and Legrain, M.J. (1983) The glutathione-dependent glyoxalase pathway in the yeast Saccharomyces cerevisiae: a vital defense line against methylglyoxal produced during glycerol catabolism. J. Biol. Chem. 258, 6030-6036.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6030-6036
    • Penninckx, M.J.1    Jaspers, C.J.2    Legrain, M.J.3
  • 25
    • 0027417473 scopus 로고
    • Cloning and characterization of human colon glyoxalase-I
    • Ranganathan, S., Walsh, E.S., Godwin, A.K. and Tew, K.D. (1993) Cloning and characterization of human colon glyoxalase-I. J. Biol. Chem. 268, 5661-5667.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5661-5667
    • Ranganathan, S.1    Walsh, E.S.2    Godwin, A.K.3    Tew, K.D.4
  • 26
    • 0022870842 scopus 로고
    • Purification and characterization of glyoxalase I from Pseudomonas putida
    • Rhee, H.-I., Murata., K. and Kimura, A. (1986) Purification and characterization of glyoxalase I from Pseudomonas putida. Biochem. Biophys. Res. Commun. 141, 993-999.
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 993-999
    • Rhee, H.-I.1    Murata, K.2    Kimura, A.3
  • 27
    • 0011395766 scopus 로고
    • Metabolism of 2-ketoaldehydes in bacteria: oxidative conversion of methylglyoxal to pyruvate by an enzyme from Pseudomonas putida
    • Rhee, H.-I., Watanabe, K., Murata, K. and Kimura, A. (1987) Metabolism of 2-ketoaldehydes in bacteria: oxidative conversion of methylglyoxal to pyruvate by an enzyme from Pseudomonas putida. Agric. Biol. Chem. 51, 1059-1066.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 1059-1066
    • Rhee, H.-I.1    Watanabe, K.2    Murata, K.3    Kimura, A.4
  • 28
    • 85004435278 scopus 로고
    • Nucleotide sequence of the glyoxalase I gene of Pseudomonas putida
    • Rhee, H.-I., Sato, N., Murata., K. and Kimura, A. (1988) Nucleotide sequence of the glyoxalase I gene of Pseudomonas putida. Agric. Biol. Chem. 52, 2243-2246.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 2243-2246
    • Rhee, H.-I.1    Sato, N.2    Murata, K.3    Kimura, A.4
  • 29
    • 0025787465 scopus 로고
    • Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance
    • Richard, J.P. (1991) Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance. Biochemistry 30, 4581-4585.
    • (1991) Biochemistry , vol.30 , pp. 4581-4585
    • Richard, J.P.1
  • 30
    • 0029866943 scopus 로고    scopus 로고
    • Optimized heterologous expression of the human zinc enzyme glyoxalase I
    • Ridderström, M. and Mannervik, B. (1996) Optimized heterologous expression of the human zinc enzyme glyoxalase I. Biochem. J. 314, 463-467.
    • (1996) Biochem. J. , vol.314 , pp. 463-467
    • Ridderström, M.1    Mannervik, B.2
  • 31
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • USA
    • Sanger, F., Nicklen, S. and Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
    • (1977) Proc. Natl. Acad. Sci. , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, A.R.3
  • 32
    • 0020479513 scopus 로고
    • Nuclear relaxation studies of the role of the essential metal in glyoxalase I
    • Sellin, S., Rosevear, P.R., Mannervik., B. and Mildvan, A.S. (1982) Nuclear relaxation studies of the role of the essential metal in glyoxalase I. J. Biol. Chem. 257, 10023-10029.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10023-10029
    • Sellin, S.1    Rosevear, P.R.2    Mannervik, B.3    Mildvan, A.S.4
  • 33
    • 0021111613 scopus 로고
    • Octahedral metal coordination in the active site of glyoxalase I as evidenced by the properties of Co(II)-glyoxalase I
    • Sellin, S., Eriksson, L.E.G., Aronsson, A.-C. and Mannervik, B. (1983) Octahedral metal coordination in the active site of glyoxalase I as evidenced by the properties of Co(II)-glyoxalase I. J. Biol. Chem. 258, 2091-2093.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2091-2093
    • Sellin, S.1    Eriksson, L.E.G.2    Aronsson, A.-C.3    Mannervik, B.4
  • 34
    • 0025298551 scopus 로고
    • The glyoxalase system: new developments towars functional characterization of a metabolic pathway fundamental to biological life
    • Thornalley, P.J. (1990) The glyoxalase system: new developments towars functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 269, 1-11.
    • (1990) Biochem. J. , vol.269 , pp. 1-11
    • Thornalley, P.J.1
  • 35
    • 0029005896 scopus 로고
    • Advances in glyoxalase research. Glyoxalase expression in malignancy, anti-proliferative effects of methylglyoxal, glyoxalase I inhibitor diesters and S-D-lactoylglutatione, and methylglyoxal-modified protein binding and endocytosis by the advanced glycation endproduct receptor
    • Thornalley, P.J. (1995) Advances in glyoxalase research. Glyoxalase expression in malignancy, anti-proliferative effects of methylglyoxal, glyoxalase I inhibitor diesters and S-D-lactoylglutatione, and methylglyoxal-modified protein binding and endocytosis by the advanced glycation endproduct receptor. Crit. Rev. Oncol./Hematol. 20, 99-128.
    • (1995) Crit. Rev. Oncol./Hematol. , vol.20 , pp. 99-128
    • Thornalley, P.J.1
  • 36
    • 0028038969 scopus 로고
    • Antimalarial activity in vitro of the glyoxalase I inhibitor diester, S-p-bromobenzylglutathione diethyl ester
    • Thornalley, P.J., Strath, M. and Wilson, R.J.M. (1994) Antimalarial activity in vitro of the glyoxalase I inhibitor diester, S-p-bromobenzylglutathione diethyl ester. Biochem. Pharmacol. 47, 418-420.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 418-420
    • Thornalley, P.J.1    Strath, M.2    Wilson, R.J.M.3
  • 38
    • 0016716116 scopus 로고
    • Growth inhibitory properties of aromatic α-ketoaldehydes toward bacteria and yeast. Comparison of inhibition and glyoxalase I activity
    • Vander Jagt, D.L. (1975) Growth inhibitory properties of aromatic α-ketoaldehydes toward bacteria and yeast. Comparison of inhibition and glyoxalase I activity. J. Med. Chem. 18, 1155-1158.
    • (1975) J. Med. Chem. , vol.18 , pp. 1155-1158
    • Vander Jagt, D.L.1
  • 39
    • 0002100821 scopus 로고
    • The Glyoxalase System
    • In: Dolphin, D., Poulsin, R. and Avramović, D. (Eds) Part A. Wiley, New York, NY
    • Vander Jagt, D.L. (1989) The Glyoxalase System. In: Dolphin, D., Poulsin, R. and Avramović, D. (Eds), Coenzymes and Cofactors VIII: Glutathione, Part A. Wiley, New York, NY, pp. 597-641.
    • (1989) Coenzymes and Cofactors VIII: Glutathione , pp. 597-641
    • Vander Jagt, D.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.