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Volumn 101, Issue 1-2, 1999, Pages 1-11

Cloning and kinetic characterization of the Trypanosoma cruzi S-adenosylmethionine decarboxylase

Author keywords

Polyamines; S adenosylmethionine decarboxylase; T. cruzi

Indexed keywords

ADENOSYLMETHIONINE DECARBOXYLASE; CADAVERINE; COMPLEMENTARY DNA; POLYAMINE; PUTRESCINE; RECOMBINANT ENZYME;

EID: 0032998601     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(98)00181-9     Document Type: Article
Times cited : (28)

References (41)
  • 2
    • 0025325255 scopus 로고
    • Molecular genetics of polyamine synthesis in eukaryotic cells
    • Heby O., Persson L. Molecular genetics of polyamine synthesis in eukaryotic cells. Trends Biochem. Sci. 15:1990;153-158.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 153-158
    • Heby, O.1    Persson, L.2
  • 3
    • 0027097783 scopus 로고
    • S-adenosylmethionine decarboxylase as an enzyme target for therapy
    • Pegg A., McCann P. S-adenosylmethionine decarboxylase as an enzyme target for therapy. Pharm. Therap. 56:1992;359-377.
    • (1992) Pharm. Therap. , vol.56 , pp. 359-377
    • Pegg, A.1    McCann, P.2
  • 4
    • 0031057528 scopus 로고    scopus 로고
    • Diamine auxotrophy may be a universal feature of Trypansoma cruzi epimastigotes
    • Ariyanayagam M., Fairlamb A. Diamine auxotrophy may be a universal feature of Trypansoma cruzi epimastigotes. Mol. Biochem. Parasitol. 84:1997;111-121.
    • (1997) Mol. Biochem. Parasitol. , vol.84 , pp. 111-121
    • Ariyanayagam, M.1    Fairlamb, A.2
  • 5
    • 0028670451 scopus 로고
    • Identification and biosynthesis of N1,N9-bis(glutathionyl)aminopropylcadaverine (homotrypanothione) in Trypanosoma cruzi
    • Hunter K., Le Quesne S., Fairlamb A. Identification and biosynthesis of N1,N9-bis(glutathionyl)aminopropylcadaverine (homotrypanothione) in Trypanosoma cruzi. Eur. J. Biochem. 226:1994;1019-1027.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 1019-1027
    • Hunter, K.1    Le Quesne, S.2    Fairlamb, A.3
  • 6
    • 0029898712 scopus 로고    scopus 로고
    • Regulation of a high affinity diamine transport system in Trypanosoma cruzi epimastigotes
    • Le Quesne S., Fairlamb A. Regulation of a high affinity diamine transport system in Trypanosoma cruzi epimastigotes. Biochem. J. 316:1996;481-486.
    • (1996) Biochem. J. , vol.316 , pp. 481-486
    • Le Quesne, S.1    Fairlamb, A.2
  • 7
    • 0027198139 scopus 로고
    • Inhibition of S-adenosyl-L-methionine (adomet) decarboxylase by the decarboxylated adomet analog 5′{[(Z)-4-amino-2-butenyl]methylamino}-5′-deoxyadenosine (MDL73811) decreases the capacities of Trypanosoma cruzi to infect and multiply within a mammalian host cell
    • Yakubu M., Majumder S., Kierszenbaum F. Inhibition of S-adenosyl-L-methionine (adomet) decarboxylase by the decarboxylated adomet analog 5′{[(Z)-4-amino-2-butenyl]methylamino}-5′-deoxyadenosine (MDL73811) decreases the capacities of Trypanosoma cruzi to infect and multiply within a mammalian host cell. J. Parasitol. 79:1993;525-532.
    • (1993) J. Parasitol. , vol.79 , pp. 525-532
    • Yakubu, M.1    Majumder, S.2    Kierszenbaum, F.3
  • 8
    • 0017708774 scopus 로고
    • Identification of a pyruvoyl residue in S-adenosylmethionine decarboxylase from Saccharomyces cerevisiae
    • Cohn M., Tabor C., Tabor H. Identification of a pyruvoyl residue in S-adenosylmethionine decarboxylase from Saccharomyces cerevisiae. J. Biol. Chem. 252:1977;8212-8216.
    • (1977) J. Biol. Chem. , vol.252 , pp. 8212-8216
    • Cohn, M.1    Tabor, C.2    Tabor, H.3
  • 9
    • 0017758520 scopus 로고
    • Evidence for the presence of pyruvate in rat liver S-adenosylmethionine decarboxylase
    • Pegg A. Evidence for the presence of pyruvate in rat liver S-adenosylmethionine decarboxylase. FEBS. Lett. 84:1977;33-36.
    • (1977) FEBS. Lett. , vol.84 , pp. 33-36
    • Pegg, A.1
  • 10
    • 0020710757 scopus 로고
    • Conversion of prohistidine decarboxylase to histidine decarboxylase: Peptide chain cleavage by nonhydrolytic serinolysis
    • Recsei P.A., Huynh Q.K., Snaee E.E. Conversion of prohistidine decarboxylase to histidine decarboxylase: peptide chain cleavage by nonhydrolytic serinolysis. PNAS. 80:1983;973-977.
    • (1983) PNAS , vol.80 , pp. 973-977
    • Recsei, P.A.1    Huynh, Q.K.2    Snaee, E.E.3
  • 11
    • 0018788360 scopus 로고
    • Purification and characterization of S-adenosyl-L-methionine decarboxylase from mouse mammary gland and liver
    • Sakai T., Hori C., Kano K., Oka T. Purification and characterization of S-adenosyl-L-methionine decarboxylase from mouse mammary gland and liver. Biochemistry. 18:1979;5541-5548.
    • (1979) Biochemistry , vol.18 , pp. 5541-5548
    • Sakai, T.1    Hori, C.2    Kano, K.3    Oka, T.4
  • 12
    • 0016764283 scopus 로고
    • S-adenosylmethionine decarboxylase from baker's yeast
    • Poso H., Sinervirta R., Janne J. S-adenosylmethionine decarboxylase from baker's yeast. Biochem. J. 151:1975;67-73.
    • (1975) Biochem. J. , vol.151 , pp. 67-73
    • Poso, H.1    Sinervirta, R.2    Janne, J.3
  • 13
    • 0015389839 scopus 로고
    • S-adenosylmethionine decarboxylase from human prostate: Activation by putrescine
    • Zappia V., Carteni-Farina M., Della Pietra G. S-adenosylmethionine decarboxylase from human prostate: activation by putrescine. Biochem. J. 129:1972;703-709.
    • (1972) Biochem. J. , vol.129 , pp. 703-709
    • Zappia, V.1    Carteni-Farina, M.2    Della Pietra, G.3
  • 14
    • 0024325586 scopus 로고
    • Activation of rat liver S-adenosylmethionine decarboxylase by putrescine and 2-substituted 1,4-butanediamines
    • Dezeure F., Gerhart F., Seiler N. Activation of rat liver S-adenosylmethionine decarboxylase by putrescine and 2-substituted 1,4-butanediamines. Int. J. Biochem. 21:1989;889-899.
    • (1989) Int. J. Biochem. , vol.21 , pp. 889-899
    • Dezeure, F.1    Gerhart, F.2    Seiler, N.3
  • 15
    • 0016604645 scopus 로고
    • Putrescine-insensitive S-adenosyl-L-methionine decarboxylase from Tetrahymena pyriformis
    • Poso H., Sinervirta R., Himberg J., Janne J. Putrescine-insensitive S-adenosyl-L-methionine decarboxylase from Tetrahymena pyriformis. Acta Chem. Scand. 29:1975;932-936.
    • (1975) Acta Chem. Scand. , vol.29 , pp. 932-936
    • Poso, H.1    Sinervirta, R.2    Himberg, J.3    Janne, J.4
  • 16
    • 0017284993 scopus 로고
    • Adenosylmethionine decarboxylase from various organisms: Relation of the putrescine activation of the enzyme to the ability of the organism to synthesize spermine
    • Poso H., Hannonen P., Himberg J., Janne J. Adenosylmethionine decarboxylase from various organisms: relation of the putrescine activation of the enzyme to the ability of the organism to synthesize spermine. Biochem. Biophys. Res. Commun. 68:1976;227-234.
    • (1976) Biochem. Biophys. Res. Commun. , vol.68 , pp. 227-234
    • Poso, H.1    Hannonen, P.2    Himberg, J.3    Janne, J.4
  • 17
    • 0026492878 scopus 로고
    • Putrescine activated S-adenosylmethionine decarboxylase from Trypanosoma brucei brucei
    • Tekwani B., Bacchi C., Pegg A. Putrescine activated S-adenosylmethionine decarboxylase from Trypanosoma brucei brucei. Mol. Cell. Biochem. 117:1992;53-61.
    • (1992) Mol. Cell. Biochem. , vol.117 , pp. 53-61
    • Tekwani, B.1    Bacchi, C.2    Pegg, A.3
  • 18
    • 0022454288 scopus 로고
    • Characterization of Trypanosoma brucei brucei S-adenosyl-L-methionine decarboxylase and its inhibition by berenil, pentamidine and methylglyoxal bis (guanylhydrazone)
    • Bitonti A., Dumont J., McCann P. Characterization of Trypanosoma brucei brucei S-adenosyl-L-methionine decarboxylase and its inhibition by berenil, pentamidine and methylglyoxal bis (guanylhydrazone). Biochem. J. 237:1986;685-689.
    • (1986) Biochem. J. , vol.237 , pp. 685-689
    • Bitonti, A.1    Dumont, J.2    McCann, P.3
  • 19
    • 0026738158 scopus 로고
    • Irreversible inhibition of S-adenosylmethionine decarboxylase of Trypanosoma brucei brucei by S-adenosylmethionine analogs
    • Tekwani B., Bacchi C., Secrist J., Pegg A. Irreversible inhibition of S-adenosylmethionine decarboxylase of Trypanosoma brucei brucei by S-adenosylmethionine analogs. Biochem. Pharmacol. 44:1992;905-911.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 905-911
    • Tekwani, B.1    Bacchi, C.2    Secrist, J.3    Pegg, A.4
  • 21
    • 0027350856 scopus 로고
    • Culturing and biological cloning of Trypanosoma cruzi
    • In: Hyde JE, editor NJ: Humana Press
    • Miles MA. Culturing and biological cloning of Trypanosoma cruzi. In: Hyde JE, editor. Protocols in Molecular Parasitology. Methods in Molecular Biology, Vol. 21. NJ: Humana Press, 1993, pp. 15-28.
    • (1993) Protocols in Molecular Parasitology. Methods in Molecular Biology , vol.21 , pp. 15-28
    • Miles, M.A.1
  • 22
    • 0030016346 scopus 로고    scopus 로고
    • Characterization of Trypanosoma brucei γ-glutamylcysteine synthetase, an essential enzyme in the biosynthesis of trypanothione
    • Lueder D., Phillips M. Characterization of Trypanosoma brucei γ-glutamylcysteine synthetase, an essential enzyme in the biosynthesis of trypanothione. J. Biol. Chem. 271:1996;17485-17490.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17485-17490
    • Lueder, D.1    Phillips, M.2
  • 23
    • 0028067923 scopus 로고
    • Formation of functional cross-species heterodimers of ornithine decarboxylase
    • Osterman A., Grishin N., Kinch L., Phillips M. Formation of functional cross-species heterodimers of ornithine decarboxylase. Biochemistry. 33:1994;13662-13667.
    • (1994) Biochemistry , vol.33 , pp. 13662-13667
    • Osterman, A.1    Grishin, N.2    Kinch, L.3    Phillips, M.4
  • 24
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S., von Hippel P. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.1    Von Hippel, P.2
  • 25
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:1987;10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 26
    • 0020643519 scopus 로고
    • S-Adenosylmethionine decarboxylase (rat liver)
    • In: Tabor H, Tabor CW, editors Academic Press
    • Pegg A, Poso H. S-Adenosylmethionine decarboxylase (rat liver). In: Tabor H, Tabor CW, editors. Methods in enzymology, 94th ed. Academic Press, 1983, pp. 234-239.
    • (1983) Methods in Enzymology, 94th Ed. , pp. 234-239
    • Pegg, A.1    Poso, H.2
  • 27
    • 0003518480 scopus 로고
    • John Wiley and Sons, New York
    • Segel IH. Enzyme Kinetics, John Wiley and Sons, New York, 1975.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 28
    • 0024999490 scopus 로고
    • Irreversible inhibition of rat S-adenosylmethionine decarboxylase by 5′-([(Z)-4-amino-2-butenyl]methylamino)-5′-deoxyadenosine
    • Danzin C., Marchal P., Casara P. Irreversible inhibition of rat S-adenosylmethionine decarboxylase by 5′-([(Z)-4-amino-2-butenyl]methylamino)-5′-deoxyadenosine. Biochem. Pharmacol. 40:1990;1499-1503.
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 1499-1503
    • Danzin, C.1    Marchal, P.2    Casara, P.3
  • 30
    • 0024450303 scopus 로고
    • Characterization of the spliced leader genes and transcripts in Trypanosoma cruzi
    • McCarthy-Burke C., Taylor Z.A., Buck G. Characterization of the spliced leader genes and transcripts in Trypanosoma cruzi. Gene. 82:1989;177-189.
    • (1989) Gene , vol.82 , pp. 177-189
    • McCarthy-Burke, C.1    Taylor, Z.A.2    Buck, G.3
  • 31
    • 0026015245 scopus 로고
    • Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity
    • Stanley B., Pegg A. Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity. J. Biol. Chem. 266:1991;18502-18506.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18502-18506
    • Stanley, B.1    Pegg, A.2
  • 32
    • 0028309730 scopus 로고
    • Expression of mammalian S-adenosylmethionine decarboxylase in Escherichia coli: Determination of sites for putrescine activation of activity and processing
    • Stanley B., Shantz L., Pegg A. Expression of mammalian S-adenosylmethionine decarboxylase in Escherichia coli: determination of sites for putrescine activation of activity and processing. J. Biol. Chem. 269:1994;7901-7907.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7901-7907
    • Stanley, B.1    Shantz, L.2    Pegg, A.3
  • 33
    • 0030695934 scopus 로고    scopus 로고
    • Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes
    • Xiong H., Stanley B., Tekwani B., Pegg A. Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes. J. Biol. Chem. 272:1997;28342-28348.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28342-28348
    • Xiong, H.1    Stanley, B.2    Tekwani, B.3    Pegg, A.4
  • 34
    • 0026684203 scopus 로고
    • Purification of human S-adenosylmethionine decarboxylase expressed in Escherichia coli and use of this protein to investigate the mechanism of inhibition by the irreversible inhibitors, 5′-deoxy-5′-[(3-hydrazinopropyl)methylamino]adenosine and 5′-([(Z)-4-amino-2-butenyl]methylamino)-5′-deoxyadenosine
    • Shantz L., Stanley B., Secrist J.I., Pegg A. Purification of human S-adenosylmethionine decarboxylase expressed in Escherichia coli and use of this protein to investigate the mechanism of inhibition by the irreversible inhibitors, 5′-deoxy-5′-[(3-hydrazinopropyl)methylamino]adenosine and 5′-([(Z)-4-amino-2-butenyl]methylamino)-5′-deoxyadenosine. Biochemistry. 31:1992;6848-6855.
    • (1992) Biochemistry , vol.31 , pp. 6848-6855
    • Shantz, L.1    Stanley, B.2    Secrist, J.I.3    Pegg, A.4
  • 35
    • 0028071521 scopus 로고
    • Role of the 5′-untranslated region of mRNA in the synthesis of S-adenosylmethionine decarboxylase and its regulation by spermine
    • Shantz L., Viswanath R., Pegg A. Role of the 5′-untranslated region of mRNA in the synthesis of S-adenosylmethionine decarboxylase and its regulation by spermine. Biochem. J. 302:1994;65-772.
    • (1994) Biochem. J. , vol.302 , pp. 65-772
    • Shantz, L.1    Viswanath, R.2    Pegg, A.3
  • 36
    • 0027510121 scopus 로고
    • Cell-specific translational regulation of S-adenosylmethionine decarboxylase mRNA
    • Hill J.R., Morris D.R. Cell-specific translational regulation of S-adenosylmethionine decarboxylase mRNA. J. Biol. Chem. 268:1993;726-731.
    • (1993) J. Biol. Chem. , vol.268 , pp. 726-731
    • Hill, J.R.1    Morris, D.R.2
  • 37
    • 0028985119 scopus 로고
    • CDNAs for S-adenosyl-L-methionine decarboxylase from Catharanthus roseus, heterologous expression, identification of the proenzyme-processing site, evidence for the presence of both subunits in the active enzyme, and a conserved region in the 5′ mRNA leader
    • Schroder G., Schroder J. cDNAs for S-adenosyl-L-methionine decarboxylase from Catharanthus roseus, heterologous expression, identification of the proenzyme-processing site, evidence for the presence of both subunits in the active enzyme, and a conserved region in the 5′ mRNA leader. Eur. J. Biochem. 228:1995;74-78.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 74-78
    • Schroder, G.1    Schroder, J.2
  • 38
    • 0027438385 scopus 로고
    • S-adenosyl-methionine decarboxylase of Acanthamoeba catellanii (Neff): Purification and properties
    • Hugo E.R., Byers T.J. S-adenosyl-methionine decarboxylase of Acanthamoeba catellanii (Neff): purification and properties. Biochem. J. 295:1993;203-309.
    • (1993) Biochem. J. , vol.295 , pp. 203-309
    • Hugo, E.R.1    Byers, T.J.2
  • 39
    • 0029853782 scopus 로고    scopus 로고
    • A novel trans-spliced mRNA from Oncocerca volvulus encodes a functional S-adenosylmethionine decarboxylase
    • Da'Dara A.A., Henkle-Dursen K., Walter R.D. A novel trans-spliced mRNA from Oncocerca volvulus encodes a functional S-adenosylmethionine decarboxylase. Biochem. J. 320:1996;519-530.
    • (1996) Biochem. J. , vol.320 , pp. 519-530
    • Da'Dara, A.A.1    Henkle-Dursen, K.2    Walter, R.D.3
  • 40
    • 0026033857 scopus 로고
    • Antitrypanosomal effects of polyamine biosnythesis inhibitors correlate with increases in Trypanosoma brucei S-adenosyl-L-methionine
    • Byers T.L., Bush T.L., McCann P.P., Bitonti A.J. Antitrypanosomal effects of polyamine biosnythesis inhibitors correlate with increases in Trypanosoma brucei S-adenosyl-L-methionine. Biochem. J. 274:1991;527-533.
    • (1991) Biochem. J. , vol.274 , pp. 527-533
    • Byers, T.L.1    Bush, T.L.2    McCann, P.P.3    Bitonti, A.J.4
  • 41
    • 0032143330 scopus 로고    scopus 로고
    • Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase: Characterization of the gene and the encoded enzyme
    • Pearsson K., Aslund L., Grahn B., Hanke J., Heby O. Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase: characterization of the gene and the encoded enzyme. Biochem. J. 333:1998;527-537.
    • (1998) Biochem. J. , vol.333 , pp. 527-537
    • Pearsson, K.1    Aslund, L.2    Grahn, B.3    Hanke, J.4    Heby, O.5


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