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Volumn 141, Issue 4, 2007, Pages 535-544

Structure of the antitumour enzyme L-methionine γ-lyase from Pseudomonas putida at 1.8 Å resolution

Author keywords

L methionine lyase; Pyridoxal 5 phosphate; X ray structure

Indexed keywords

ARGININE; CYSTEINE; LYSINE; METHIONINE GAMMA LYASE; TYROSINE; L-METHIONINE GAMMA-LYASE; LYASE; UNCLASSIFIED DRUG;

EID: 38149061604     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm055     Document Type: Article
Times cited : (68)

References (37)
  • 1
    • 0032836048 scopus 로고    scopus 로고
    • Pathways of assimilative sulfur metabolism in Pseudomonas putida
    • Vermeij, P. and Kertesz, M.A. (1999) Pathways of assimilative sulfur metabolism in Pseudomonas putida. J. Bacteriol. 181, 5833-5837
    • (1999) J. Bacteriol , vol.181 , pp. 5833-5837
    • Vermeij, P.1    Kertesz, M.A.2
  • 2
    • 0031008473 scopus 로고    scopus 로고
    • Molecular characterization of the mde operon involved in L-methionine catabolism of Pseudomonas putida
    • Inoue, H., Inagaki, K., Eriguchi, S., Tamura, T., Esaki, N., Soda, K., and Tanaka, H. (1997) Molecular characterization of the mde operon involved in L-methionine catabolism of Pseudomonas putida. J. Bacteriol. 179, 3956-3962
    • (1997) J. Bacteriol , vol.179 , pp. 3956-3962
    • Inoue, H.1    Inagaki, K.2    Eriguchi, S.3    Tamura, T.4    Esaki, N.5    Soda, K.6    Tanaka, H.7
  • 3
    • 0017580979 scopus 로고
    • Properties of L-methionine γ-lyase from Pseudomonas ovalis
    • Tanaka, H., Esaki, N., and Soda, K. (1977) Properties of L-methionine γ-lyase from Pseudomonas ovalis. Biochemistry 16, 100-106
    • (1977) Biochemistry , vol.16 , pp. 100-106
    • Tanaka, H.1    Esaki, N.2    Soda, K.3
  • 4
    • 0025947233 scopus 로고
    • Purification and characterization of methionine γ-lyase from Trichomonas vaginalis
    • Lockwood, B.C. and Coombs, G.H. (1991) Purification and characterization of methionine γ-lyase from Trichomonas vaginalis. Biochem. J. 279, 675-682
    • (1991) Biochem. J , vol.279 , pp. 675-682
    • Lockwood, B.C.1    Coombs, G.H.2
  • 5
    • 0142180049 scopus 로고    scopus 로고
    • Identification and characterization of two isoenzymes of methionine γ-lyase from Entamoeba histolytica: A key enzyme of sulfur-amino acid degradation in an anaerobic parasitic protist that lacks forward and reverse trans-sulfuration pathways
    • Tokoro, M., Asai, T., Kobayashi, S., Takeuchi, T., and Nozaki, T. (2003) Identification and characterization of two isoenzymes of methionine γ-lyase from Entamoeba histolytica: a key enzyme of sulfur-amino acid degradation in an anaerobic parasitic protist that lacks forward and reverse trans-sulfuration pathways. J. Biol. Chem. 278, 42717-42727
    • (2003) J. Biol. Chem , vol.278 , pp. 42717-42727
    • Tokoro, M.1    Asai, T.2    Kobayashi, S.3    Takeuchi, T.4    Nozaki, T.5
  • 6
    • 0021202606 scopus 로고
    • Purification and properties of L-methionine γ-lyase from Aeromonas sp
    • Nakayama, T., Esaki, N., Lee, W.J., Tanaka, I., Tanaka, H., and Soda, K. (1984) Purification and properties of L-methionine γ-lyase from Aeromonas sp. Agric. Biol. Chem. 48, 2367-2369
    • (1984) Agric. Biol. Chem , vol.48 , pp. 2367-2369
    • Nakayama, T.1    Esaki, N.2    Lee, W.J.3    Tanaka, I.4    Tanaka, H.5    Soda, K.6
  • 7
    • 18944395885 scopus 로고    scopus 로고
    • A gene encoding L-methionine γ-lyase is present in Enterobacteriaceae family genomes: Identification and characterization of Citrobacter freundii L-methionine γ-lyase
    • Manukhov, I.V., Mamaeva, D.V., Rastorguev, S.M., Faleev, N.G., Morozova, E.A., Demidkina, T.V., and Zavilgelsky, G.B. (2005) A gene encoding L-methionine γ-lyase is present in Enterobacteriaceae family genomes: identification and characterization of Citrobacter freundii L-methionine γ-lyase. J. Bacteriol. 187, 3889-3893
    • (2005) J. Bacteriol , vol.187 , pp. 3889-3893
    • Manukhov, I.V.1    Mamaeva, D.V.2    Rastorguev, S.M.3    Faleev, N.G.4    Morozova, E.A.5    Demidkina, T.V.6    Zavilgelsky, G.B.7
  • 8
    • 10444290571 scopus 로고    scopus 로고
    • Identification and functional analysis of the gene encoding methionine γ-lyase in Brevibacterium linens
    • Amarita, F., Yvon, M., Nardi, M., Chambellon, E., Delettre, J., and Bonnarme, P. (2004) Identification and functional analysis of the gene encoding methionine γ-lyase in Brevibacterium linens. Appl. Environ. Microbiol. 70, 7348-7354
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 7348-7354
    • Amarita, F.1    Yvon, M.2    Nardi, M.3    Chambellon, E.4    Delettre, J.5    Bonnarme, P.6
  • 9
    • 0034440801 scopus 로고    scopus 로고
    • Formation of methyl mercaptan from L-methionine by Porphyromonas gingivalis
    • Yoshimura, M., Nakano, Y., Yamashita, Y., Oho, T., Saito, T., and Koga, T. (2000) Formation of methyl mercaptan from L-methionine by Porphyromonas gingivalis. Infect. Immun. 68, 6912-6916
    • (2000) Infect. Immun , vol.68 , pp. 6912-6916
    • Yoshimura, M.1    Nakano, Y.2    Yamashita, Y.3    Oho, T.4    Saito, T.5    Koga, T.6
  • 10
    • 17444365031 scopus 로고    scopus 로고
    • High production of methyl mercaptan by L-methionine-alpha- deamino-gamma-mercaptomethane lyase from Treponema denticola
    • Fukamachi, H., Nakano, Y., Okano, S., Shibata, Y., Abiko, Y., and Yamashita, Y. (2005) High production of methyl mercaptan by L-methionine-alpha- deamino-gamma-mercaptomethane lyase from Treponema denticola. Biochem. Biophys. Res. Commun. 331, 127-131
    • (2005) Biochem. Biophys. Res. Commun , vol.331 , pp. 127-131
    • Fukamachi, H.1    Nakano, Y.2    Okano, S.3    Shibata, Y.4    Abiko, Y.5    Yamashita, Y.6
  • 14
    • 0031106365 scopus 로고    scopus 로고
    • Overexpression and large-scale production of recombinant L-methionine-α-deamino-γ-mercaptomethane-lyase for novel anticancer therapy
    • Tan, Y., Xu, M., Tan, X., Wang, X., Saikawa, Y., Nagahama, T., Sun, X., Lenz, M., and Hoffman, R.M. (1997) Overexpression and large-scale production of recombinant L-methionine-α-deamino-γ-mercaptomethane-lyase for novel anticancer therapy. Protein Expr. Purif. 9, 233-245
    • (1997) Protein Expr. Purif , vol.9 , pp. 233-245
    • Tan, Y.1    Xu, M.2    Tan, X.3    Wang, X.4    Saikawa, Y.5    Nagahama, T.6    Sun, X.7    Lenz, M.8    Hoffman, R.M.9
  • 22
    • 1642421062 scopus 로고    scopus 로고
    • Assay method for antitumor L-methionine γ-lyase: Comprehensive kinetic analysis of the complex reaction with L-methionine
    • Takakura, T., Mitsushima, K., Yagi, S., Inagaki, K., Tanaka, H., Esaki, N., Soda, K., and Takimoto, A. (2004) Assay method for antitumor L-methionine γ-lyase: comprehensive kinetic analysis of the complex reaction with L-methionine. Anal. Biochem. 327, 233-240
    • (2004) Anal. Biochem , vol.327 , pp. 233-240
    • Takakura, T.1    Mitsushima, K.2    Yagi, S.3    Inagaki, K.4    Tanaka, H.5    Esaki, N.6    Soda, K.7    Takimoto, A.8
  • 24
    • 0030595364 scopus 로고    scopus 로고
    • Crystal structure of the pyridoxal-5′-phosphate dependent cystathionine β-lyase from Escherichia coli at 1.83Å
    • Clausen, T., Huber, R., Laber, B., Pohlenz, H.D., and Messerschmidt, A. (1996) Crystal structure of the pyridoxal-5′-phosphate dependent cystathionine β-lyase from Escherichia coli at 1.83Å. J. Mol. Biol. 262, 202-224
    • (1996) J. Mol. Biol , vol.262 , pp. 202-224
    • Clausen, T.1    Huber, R.2    Laber, B.3    Pohlenz, H.D.4    Messerschmidt, A.5
  • 25
    • 0018793933 scopus 로고
    • Suicide inactivation of bacterial cystathionine γ-synthase and methionine γ-lyase during processing of L-propargylglycine
    • Johnston, M., Jankowski, D., Marcotte, P., Tanaka, H., Esaki, N., Soda, K., and Walsh, C. (1979) Suicide inactivation of bacterial cystathionine γ-synthase and methionine γ-lyase during processing of L-propargylglycine. Biochemistry 18, 4690-4701
    • (1979) Biochemistry , vol.18 , pp. 4690-4701
    • Johnston, M.1    Jankowski, D.2    Marcotte, P.3    Tanaka, H.4    Esaki, N.5    Soda, K.6    Walsh, C.7
  • 26
    • 0037133543 scopus 로고    scopus 로고
    • Modulation of the internal aldimine pKa's of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues
    • Eliot, A.C. and Kirsch, J.F. (2002) Modulation of the internal aldimine pKa's of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues. Biochemistry 41, 3836-3842
    • (2002) Biochemistry , vol.41 , pp. 3836-3842
    • Eliot, A.C.1    Kirsch, J.F.2
  • 27
    • 0032402991 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli cystathionine γ-synthase at 1.5Å resolution
    • Clausen, T., Huber, R., Prade, L., Wahl, M.C., and Messerschmidt, A. (1998) Crystal structure of Escherichia coli cystathionine γ-synthase at 1.5Å resolution. EMBO J. 17, 6827-6838
    • (1998) EMBO J , vol.17 , pp. 6827-6838
    • Clausen, T.1    Huber, R.2    Prade, L.3    Wahl, M.C.4    Messerschmidt, A.5
  • 28
    • 0025270921 scopus 로고
    • Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase
    • Hayashi, H., Inoue, Y., Kuramitsu, S., Morino, Y., and Kagamiyama, H. (1990) Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase. Biochem. Biophys. Res. Commun. 167, 407-412
    • (1990) Biochem. Biophys. Res. Commun , vol.167 , pp. 407-412
    • Hayashi, H.1    Inoue, Y.2    Kuramitsu, S.3    Morino, Y.4    Kagamiyama, H.5
  • 30
    • 85004625108 scopus 로고
    • Chemical modification of cysteine residues of L-methionine γ-lyase
    • Nakayama, T., Esaki, N., Tanaka, H., and Soda, K. (1988) Chemical modification of cysteine residues of L-methionine γ-lyase. Agric. Biol. Chem. 52, 177-183
    • (1988) Agric. Biol. Chem , vol.52 , pp. 177-183
    • Nakayama, T.1    Esaki, N.2    Tanaka, H.3    Soda, K.4
  • 31
    • 0038743268 scopus 로고    scopus 로고
    • Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: Crystal structure of cystathionine γ-lyase from yeast and intrafamiliar structure comparison
    • Messerschmidt, A., Worbs, M., Steegborn, C., Wahl, M.C., Huber, R., Laber, B., and Clausen, T. (2003) Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: crystal structure of cystathionine γ-lyase from yeast and intrafamiliar structure comparison. J. Biol. Chem. 384, 373-386
    • (2003) J. Biol. Chem , vol.384 , pp. 373-386
    • Messerschmidt, A.1    Worbs, M.2    Steegborn, C.3    Wahl, M.C.4    Huber, R.5    Laber, B.6    Clausen, T.7
  • 32
    • 0029010760 scopus 로고
    • Structural analysis of the L-methionine γ-lyase gene from Pseudomonas putida
    • Inoue, H., Inagaki, K., Sugimoto, M., Esaki, N., Soda, K., and Tanaka, H. (1995) Structural analysis of the L-methionine γ-lyase gene from Pseudomonas putida. J. Biochem. 117, 1120-1125
    • (1995) J. Biochem , vol.117 , pp. 1120-1125
    • Inoue, H.1    Inagaki, K.2    Sugimoto, M.3    Esaki, N.4    Soda, K.5    Tanaka, H.6
  • 33
    • 0031662724 scopus 로고    scopus 로고
    • Purification and characterization of L-methionine γ-lyase from Brevibacterium linens BL2
    • Dias, B. and Weimer, B. (1998) Purification and characterization of L-methionine γ-lyase from Brevibacterium linens BL2. Appl. Environ. Microbiol. 64, 3327-3331
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 3327-3331
    • Dias, B.1    Weimer, B.2
  • 34
    • 0020951126 scopus 로고
    • Altered methionine metabolism, DNA methylation and oncogene expression in carcinogenesis: A review and synthesis
    • Hoffman, R.M. (1984) Altered methionine metabolism, DNA methylation and oncogene expression in carcinogenesis: a review and synthesis. Biochim. Biophys. Acta 738, 49-87
    • (1984) Biochim. Biophys. Acta , vol.738 , pp. 49-87
    • Hoffman, R.M.1
  • 35
    • 0021748312 scopus 로고
    • Hypomethylation of DNA in human cancer cells: A site-specific change in the c-myc oncogene
    • Cheah, M.S., Wallace, C.D., and Hoffman, R.M. (1984) Hypomethylation of DNA in human cancer cells: a site-specific change in the c-myc oncogene. J. Natl. Cancer Inst. 73, 1057-1065
    • (1984) J. Natl. Cancer Inst , vol.73 , pp. 1057-1065
    • Cheah, M.S.1    Wallace, C.D.2    Hoffman, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.