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Volumn 333, Issue 3, 2003, Pages 573-585

Tertiary structure of thiopurine methyltransferase from Pseudomonas syringae, a bacterial orthologue of a polymorphic, drug-metabolizing enzyme

Author keywords

Drug metabolism; Methyltransferase; NMR; S adenosylmethionine; Tertiary structure

Indexed keywords

DRUG METABOLIZING ENZYME; ENZYME; MERCAPTOPURINE; METHYLTRANSFERASE; S ADENOSYLMETHIONINE; THIOPURINE METHYLTRANSFERASE;

EID: 0141527466     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.08.039     Document Type: Article
Times cited : (29)

References (37)
  • 1
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • Martin J.L., McMillan F.M. SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr. Opin. Struct. Biol. 12:2002;783-793.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 2
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • Kagan R.M., Clarke S. Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes. Arch. Biochem. Biophys. 310:1994;417-427.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 3
    • 0035056404 scopus 로고    scopus 로고
    • Thiopurine pharmacogenetics: Clinical and molecular studies of thiopurine methyltransferase
    • Weinshilboum R. Thiopurine pharmacogenetics: clinical and molecular studies of thiopurine methyltransferase. Drug Metab. Dispos. 29:2001;601-605.
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 601-605
    • Weinshilboum, R.1
  • 4
    • 0033828949 scopus 로고    scopus 로고
    • Genetic polymorphism of thiopurine S-methyltransferase: Molecular mechanisms and clinical importance
    • Krynetski E.Y., Evans W.E. Genetic polymorphism of thiopurine S-methyltransferase: molecular mechanisms and clinical importance. Pharmacology. 61:2000;136-146.
    • (2000) Pharmacology , vol.61 , pp. 136-146
    • Krynetski, E.Y.1    Evans, W.E.2
  • 5
    • 0035755993 scopus 로고    scopus 로고
    • Recent advances in the pharmacogenomics of thiopurine methyltransferase
    • Coulthard S.A., Hall A.G. Recent advances in the pharmacogenomics of thiopurine methyltransferase. Pharmacogenomics J. 1:2001;254-261.
    • (2001) Pharmacogenomics J. , vol.1 , pp. 254-261
    • Coulthard, S.A.1    Hall, A.G.2
  • 6
    • 0018822866 scopus 로고
    • Mercaptopurine pharmacogenetics: Monogenic inheritance of erythrocyte thiopurine methyltransferase activity
    • Weinshilboum R.M., Sladek S.L. Mercaptopurine pharmacogenetics: monogenic inheritance of erythrocyte thiopurine methyltransferase activity. Am. J. Hum. Genet. 32:1980;651-662.
    • (1980) Am. J. Hum. Genet. , vol.32 , pp. 651-662
    • Weinshilboum, R.M.1    Sladek, S.L.2
  • 7
    • 0027524983 scopus 로고
    • Congenital thiopurine methyltransferase deficiency and 6-mercaptopurine toxicity during treatment for acute lymphoblastic leukaemia
    • Lennard L., Gibson B.E., Nicole T., Lilleyman J.S. Congenital thiopurine methyltransferase deficiency and 6-mercaptopurine toxicity during treatment for acute lymphoblastic leukaemia. Arch. Dis. Child. 69:1993;577-579.
    • (1993) Arch. Dis. Child , vol.69 , pp. 577-579
    • Lennard, L.1    Gibson, B.E.2    Nicole, T.3    Lilleyman, J.S.4
  • 8
    • 0025837127 scopus 로고
    • Altered mercaptopurine metabolism, toxic effects, and dosage requirement in a thiopurine methyltransferase-deficient child with acute lymphocytic leukemia
    • Evans W.E., Horner M., Chu Y.Q., Kalwinsky D., Roberts W.M. Altered mercaptopurine metabolism, toxic effects, and dosage requirement in a thiopurine methyltransferase-deficient child with acute lymphocytic leukemia. J. Pediatr. 119:1991;985-989.
    • (1991) J. Pediatr. , vol.119 , pp. 985-989
    • Evans, W.E.1    Horner, M.2    Chu, Y.Q.3    Kalwinsky, D.4    Roberts, W.M.5
  • 9
    • 0025357147 scopus 로고
    • Mouse thiopurine methyltransferase pharmacogenetics: Correlation of immunoreactive protein and enzymatic activity
    • Hernandez J.S., Van Loon J.A., Otterness D.M., Weinshilboum R.M. Mouse thiopurine methyltransferase pharmacogenetics: correlation of immunoreactive protein and enzymatic activity. J. Pharmacol. Exp. Ther. 252:1990;568-573.
    • (1990) J. Pharmacol. Exp. Ther. , vol.252 , pp. 568-573
    • Hernandez, J.S.1    Van Loon, J.A.2    Otterness, D.M.3    Weinshilboum, R.M.4
  • 10
    • 0032693405 scopus 로고    scopus 로고
    • Enhanced proteasomal degradation of mutant human thiopurine S-methyltransferase (TPMT) in mammalian cells: Mechanism for TPMT protein deficiency inherited by TPMT*2, TPMT*3A, TPMT*3B or TPMT*3C
    • Tai H.L., Fessing M.Y., Bonten E.J., Yanishevsky Y., d'Azzo A., Krynetski E.Y., Evans W.E. Enhanced proteasomal degradation of mutant human thiopurine S-methyltransferase (TPMT) in mammalian cells: mechanism for TPMT protein deficiency inherited by TPMT*2, TPMT*3A, TPMT*3B or TPMT*3C Pharmacogenetics. 9:1999;641-650.
    • (1999) Pharmacogenetics , vol.9 , pp. 641-650
    • Tai, H.L.1    Fessing, M.Y.2    Bonten, E.J.3    Yanishevsky, Y.4    D'Azzo, A.5    Krynetski, E.Y.6    Evans, W.E.7
  • 11
    • 0030986251 scopus 로고    scopus 로고
    • Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2): Mechanisms for the genetic polymorphism of TPMT activity
    • Tai H.L., Krynetski E.Y., Schuetz E.G., Yanishevski Y., Evans W.E. Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2): mechanisms for the genetic polymorphism of TPMT activity. Proc. Natl Acad. Sci. USA. 94:1997;6444-6449.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6444-6449
    • Tai, H.L.1    Krynetski, E.Y.2    Schuetz, E.G.3    Yanishevski, Y.4    Evans, W.E.5
  • 12
    • 0034663361 scopus 로고    scopus 로고
    • Purification and properties of multiple isoforms of a novel thiol methyltransferase involved in the production of volatile sulfur compounds from Brassica oleracea
    • Attieh J., Sparace S.A., Saini H.S. Purification and properties of multiple isoforms of a novel thiol methyltransferase involved in the production of volatile sulfur compounds from Brassica oleracea. Arch. Biochem. Biophys. 380:2000;257-266.
    • (2000) Arch. Biochem. Biophys. , vol.380 , pp. 257-266
    • Attieh, J.1    Sparace, S.A.2    Saini, H.S.3
  • 13
    • 0032571849 scopus 로고    scopus 로고
    • A tellurite-resistance genetic determinant from phytopathogenic pseudomonads encodes a thiopurine methyltransferase: Evidence of a widely-conserved family of methyltransferases
    • Cournoyer B., Watanabe S., Vivian A. A tellurite-resistance genetic determinant from phytopathogenic pseudomonads encodes a thiopurine methyltransferase: evidence of a widely-conserved family of methyltransferases. Biochim. Biophys. Acta. 1397:1998;161-168.
    • (1998) Biochim. Biophys. Acta , vol.1397 , pp. 161-168
    • Cournoyer, B.1    Watanabe, S.2    Vivian, A.3
  • 14
    • 0032546420 scopus 로고    scopus 로고
    • Structure, function and physiological role of glycine N-methyltransferase
    • Ogawa H., Gomi T., Takusagawa F., Fujioka M. Structure, function and physiological role of glycine N-methyltransferase. Int. J. Biochem. Cell Biol. 30:1998;13-26.
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 13-26
    • Ogawa, H.1    Gomi, T.2    Takusagawa, F.3    Fujioka, M.4
  • 15
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P., Mumenthaler C., Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273:1997;283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 16
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T., Guntert P., Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319:2002;209-227.
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 17
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR. 13:1999;289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 18
  • 19
    • 0037020195 scopus 로고    scopus 로고
    • Structures of SET domain proteins: Protein lysine methyltransferases make their mark
    • Yeates T.O. Structures of SET domain proteins: protein lysine methyltransferases make their mark. Cell. 111:2002;5-7.
    • (2002) Cell , vol.111 , pp. 5-7
    • Yeates, T.O.1
  • 20
    • 0036774065 scopus 로고    scopus 로고
    • The structure of the RlmB 23 S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot
    • Michel G., Sauve V., Larocque R., Li Y., Matte A., Cygler M. The structure of the RlmB 23 S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot. Structure (Camb.). 10:2002;1303-1315.
    • (2002) Structure (Camb.) , vol.10 , pp. 1303-1315
    • Michel, G.1    Sauve, V.2    Larocque, R.3    Li, Y.4    Matte, A.5    Cygler, M.6
  • 21
    • 0028210328 scopus 로고
    • Crystal structure of catechol O-methyltransferase
    • Vidgren J., Svensson L.A., Liljas A. Crystal structure of catechol O-methyltransferase. Nature. 368:1994;354-358.
    • (1994) Nature , vol.368 , pp. 354-358
    • Vidgren, J.1    Svensson, L.A.2    Liljas, A.3
  • 22
    • 0029787565 scopus 로고    scopus 로고
    • Crystal structure of glycine N-methyltransferase from rat liver
    • Fu Z., Hu Y., Konishi K., Takata Y., Ogawa H., Gomi T., et al. Crystal structure of glycine N-methyltransferase from rat liver. Biochemistry. 35:1996;11985-11993.
    • (1996) Biochemistry , vol.35 , pp. 11985-11993
    • Fu, Z.1    Hu, Y.2    Konishi, K.3    Takata, Y.4    Ogawa, H.5    Gomi, T.6
  • 23
    • 0034798636 scopus 로고    scopus 로고
    • Getting the adrenaline going: Crystal structure of the adrenaline-synthesizing enzyme PNMT
    • Martin J.L., Begun J., McLeish M.J., Caine J.M., Grunewald G.L. Getting the adrenaline going: crystal structure of the adrenaline-synthesizing enzyme PNMT. Structure (Camb.). 9:2001;977-985.
    • (2001) Structure (Camb.) , vol.9 , pp. 977-985
    • Martin, J.L.1    Begun, J.2    McLeish, M.J.3    Caine, J.M.4    Grunewald, G.L.5
  • 24
    • 0034812118 scopus 로고    scopus 로고
    • Two polymorphic forms of human histamine methyltransferase: Structural, thermal, and kinetic comparisons
    • Horton J.R., Sawada K., Nishibori M., Zhang X., Cheng X. Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons. Structure (Camb.). 9:2001;837-849.
    • (2001) Structure (Camb.) , vol.9 , pp. 837-849
    • Horton, J.R.1    Sawada, K.2    Nishibori, M.3    Zhang, X.4    Cheng, X.5
  • 25
    • 0036298629 scopus 로고    scopus 로고
    • Crystal structure of guanidinoacetate methyltransferase from rat liver: A model structure of protein arginine methyltransferase
    • Komoto J., Huang Y., Takata Y., Yamada T., Konishi K., Ogawa H., et al. Crystal structure of guanidinoacetate methyltransferase from rat liver: a model structure of protein arginine methyltransferase. J. Mol. Biol. 320:2002;223-235.
    • (2002) J. Mol. Biol. , vol.320 , pp. 223-235
    • Komoto, J.1    Huang, Y.2    Takata, Y.3    Yamada, T.4    Konishi, K.5    Ogawa, H.6
  • 26
    • 0035119588 scopus 로고    scopus 로고
    • Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases
    • Zubieta C., He X.Z., Dixon R.A., Noel J.P. Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases. Nature Struct. Biol. 8:2001;271-279.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 271-279
    • Zubieta, C.1    He, X.Z.2    Dixon, R.A.3    Noel, J.P.4
  • 27
    • 0029073930 scopus 로고
    • Methylation of mercaptopurine, thioguanine, and their nucleotide metabolites by heterologously expressed human thiopurine S-methyltransferase
    • Krynetski E.Y., Krynetskaia N.F., Yanishevski Y., Evans W.E. Methylation of mercaptopurine, thioguanine, and their nucleotide metabolites by heterologously expressed human thiopurine S-methyltransferase. Mol. Pharmacol. 47:1995;1141-1147.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 1141-1147
    • Krynetski, E.Y.1    Krynetskaia, N.F.2    Yanishevski, Y.3    Evans, W.E.4
  • 31
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart D.S., Sykes B.D. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR. 4:1994;171-180.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 32
    • 34249765651 scopus 로고
    • NmrView - A computer-program for the visualization and analysis of NMR data
    • Johnson B.A., Blevins R.A. NmrView - a computer-program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:1994;603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 33
    • 0031714689 scopus 로고    scopus 로고
    • Structure calculation of biological macromolecules from NMR data
    • Guntert P. Structure calculation of biological macromolecules from NMR data. Quart. Rev. Biophys. 31:1998;145-237.
    • (1998) Quart. Rev. Biophys. , vol.31 , pp. 145-237
    • Guntert, P.1
  • 34
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 35
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 37
    • 0034141555 scopus 로고    scopus 로고
    • Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 Å resolution
    • Wang H., Boisvert D., Kim K.K., Kim R., Kim S.H. Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 Å resolution. EMBO J. 19:2000;317-323.
    • (2000) EMBO J. , vol.19 , pp. 317-323
    • Wang, H.1    Boisvert, D.2    Kim, K.K.3    Kim, R.4    Kim, S.H.5


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