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Volumn 47, Issue 17, 2008, Pages 4983-4991

Comparative kinetics of cofactor association and dissociation for the human and trypanosomal S-adenosylhomocysteine hydrolases. 2. The role of helix 18 stability

Author keywords

[No Author keywords available]

Indexed keywords

COFACTOR ASSOCIATION; COMPARATIVE KINETICS; HOLOENZYMES; HUMAN ENZYMES;

EID: 42449119732     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800175g     Document Type: Article
Times cited : (6)

References (22)
  • 3
    • 0034669468 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of S-adenosylhomocysteine hydrolase from Leishmania donovani
    • Yang, X., and Borchardt, R. T. (2000) Overexpression, purification, and characterization of S-adenosylhomocysteine hydrolase from Leishmania donovani. Arch. Biochem. Biophys. 383, 272-280.
    • (2000) Arch. Biochem. Biophys , vol.383 , pp. 272-280
    • Yang, X.1    Borchardt, R.T.2
  • 4
    • 0028292569 scopus 로고
    • Plasmodium falciparum S-adenosylhomocysteine hydrolase. cDNA identification, predicted protein sequence, and expression in Escherichia coli
    • Creedon, K. A., Rathod, P. K., and Wellems, T. E. (1994) Plasmodium falciparum S-adenosylhomocysteine hydrolase. cDNA identification, predicted protein sequence, and expression in Escherichia coli. J. Biol. Chem. 269, 16364-16370.
    • (1994) J. Biol. Chem , vol.269 , pp. 16364-16370
    • Creedon, K.A.1    Rathod, P.K.2    Wellems, T.E.3
  • 5
    • 1242315505 scopus 로고    scopus 로고
    • Trypanosoma cruzi: Molecular cloning and characterization of the S-adenosylhomocysteine hydrolase
    • Parker, N. B., Yang, X., Hanke, J., Mason, K. A., Schowen, R. L., Borchardt, R. T., and Yin, D. H. (2003) Trypanosoma cruzi: molecular cloning and characterization of the S-adenosylhomocysteine hydrolase. Exp. Parasitol. 105, 149-158.
    • (2003) Exp. Parasitol , vol.105 , pp. 149-158
    • Parker, N.B.1    Yang, X.2    Hanke, J.3    Mason, K.A.4    Schowen, R.L.5    Borchardt, R.T.6    Yin, D.H.7
  • 7
    • 0022658458 scopus 로고
    • Antimalarial activity of neplanocin A with perturbations in the metabolism of purines, polyamines and S-adenosylmethionine
    • Whaun, J. M., Miura, G. A., Brown, N. D., Gordon, R. K., and Chiang, P. K. (1986) Antimalarial activity of neplanocin A with perturbations in the metabolism of purines, polyamines and S-adenosylmethionine. J. Pharmacol. Exp. Ther. 236, 277-283.
    • (1986) J. Pharmacol. Exp. Ther , vol.236 , pp. 277-283
    • Whaun, J.M.1    Miura, G.A.2    Brown, N.D.3    Gordon, R.K.4    Chiang, P.K.5
  • 8
    • 0031805505 scopus 로고    scopus 로고
    • The importance of the 4′-hydroxyl hydrogen for the anti-trypanosomal and antiviral properties of (+)-5′-noraristeromycin and two 7-deaza analogues
    • Seley, K. L., Schneller, S. W., De Clercq, E., Rattendi, D., Lane, S., Bacchi, C. J., and Korba, B. (1998) The importance of the 4′-hydroxyl hydrogen for the anti-trypanosomal and antiviral properties of (+)-5′-noraristeromycin and two 7-deaza analogues. Bioorg. Med. Chem. 6, 797-801.
    • (1998) Bioorg. Med. Chem , vol.6 , pp. 797-801
    • Seley, K.L.1    Schneller, S.W.2    De Clercq, E.3    Rattendi, D.4    Lane, S.5    Bacchi, C.J.6    Korba, B.7
  • 9
    • 0037465432 scopus 로고    scopus 로고
    • Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: Transition-state stabilization and the avoidance of abortive reactions
    • Yang, X., Hu, Y., Yin, D. H., Turner, M. A., Wang, M., Borchardt, R. T., Howell, P. L., Kuczera, K., and Schowen, R. L. (2003) Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions. Biochemistry 42, 1900-1909.
    • (2003) Biochemistry , vol.42 , pp. 1900-1909
    • Yang, X.1    Hu, Y.2    Yin, D.H.3    Turner, M.A.4    Wang, M.5    Borchardt, R.T.6    Howell, P.L.7    Kuczera, K.8    Schowen, R.L.9
  • 10
    • 5144234233 scopus 로고    scopus 로고
    • Crystal structure of S-adenosyl-L-homocysteine hydrolase from the human malaria parasite Plasmodium falciparum
    • Tanaka, N., Nakanishi, M., Kusakabe, Y., Shiraiwa, K., Yabe, S., Ito, Y., Kitade, Y., and Nakamura, K. T. (2004) Crystal structure of S-adenosyl-L-homocysteine hydrolase from the human malaria parasite Plasmodium falciparum. J. Mol. Biol. 343, 1007-1017.
    • (2004) J. Mol. Biol , vol.343 , pp. 1007-1017
    • Tanaka, N.1    Nakanishi, M.2    Kusakabe, Y.3    Shiraiwa, K.4    Yabe, S.5    Ito, Y.6    Kitade, Y.7    Nakamura, K.T.8
  • 12
    • 0028081341 scopus 로고
    • A single mutation at lysine 426 of human placental S-adenosylhomocysteine hydrolase inactivates the enzyme
    • Ault-Riche, D. B., Yuan, C. S., and Borchardt, R. T. (1994) A single mutation at lysine 426 of human placental S-adenosylhomocysteine hydrolase inactivates the enzyme. J. Biol. Chem. 269, 31472-31478.
    • (1994) J. Biol. Chem , vol.269 , pp. 31472-31478
    • Ault-Riche, D.B.1    Yuan, C.S.2    Borchardt, R.T.3
  • 13
    • 0034644738 scopus 로고    scopus 로고
    • Effects of site-directed mutagenesis on structure and function of recombinant rat liver S-adenosylhomocysteine hydrolase. Crystal structure of D244E mutant enzyme
    • Komoto, J., Huang, Y., Gomi, T., Ogawa, H., Takata, Y., Fujioka, M., and Takusagawa, F. (2000) Effects of site-directed mutagenesis on structure and function of recombinant rat liver S-adenosylhomocysteine hydrolase. Crystal structure of D244E mutant enzyme. J. Biol. Chem. 275, 32147-32156.
    • (2000) J. Biol. Chem , vol.275 , pp. 32147-32156
    • Komoto, J.1    Huang, Y.2    Gomi, T.3    Ogawa, H.4    Takata, Y.5    Fujioka, M.6    Takusagawa, F.7
  • 14
    • 34248526020 scopus 로고    scopus 로고
    • Comparative kinetics of cofactor association and dissociation for the human and trypanosomal S-adenosylhomocysteine hydrolases. 1. Basic features of the association and dissociation processes
    • Li, Q.-S., Cai, S., Borchardt, R. T., Fang, J., Kuczera, K., Middaugh, C. R., and Schowen, R. L. (2007) Comparative kinetics of cofactor association and dissociation for the human and trypanosomal S-adenosylhomocysteine hydrolases. 1. Basic features of the association and dissociation processes. Biochemistry 46, 5798-5809.
    • (2007) Biochemistry , vol.46 , pp. 5798-5809
    • Li, Q.-S.1    Cai, S.2    Borchardt, R.T.3    Fang, J.4    Kuczera, K.5    Middaugh, C.R.6    Schowen, R.L.7
  • 15
    • 0027209984 scopus 로고
    • Mechanism of inactivation of S-adenosylhomocysteine hydrolase by (Z)-4′,5′- didehydro-5′-deoxy-5′-fluoroadenosine
    • Yuan, C. S., Yeh, J., Liu, S., and Borchardt, R. T. (1993) Mechanism of inactivation of S-adenosylhomocysteine hydrolase by (Z)-4′,5′- didehydro-5′-deoxy-5′-fluoroadenosine. J. Biol. Chem. 268, 17030-17037.
    • (1993) J. Biol. Chem , vol.268 , pp. 17030-17037
    • Yuan, C.S.1    Yeh, J.2    Liu, S.3    Borchardt, R.T.4
  • 16
    • 0029961930 scopus 로고    scopus 로고
    • Chemical modification and site-directed mutagenesis of cysteine residues in human placental S-adenosylhomocysteine hydrolase
    • Yuan, C. S., Ault-Riche, D. B., and Borchardt, R. T. (1996) Chemical modification and site-directed mutagenesis of cysteine residues in human placental S-adenosylhomocysteine hydrolase. J. Biol. Chem. 271, 28009-28016.
    • (1996) J. Biol. Chem , vol.271 , pp. 28009-28016
    • Yuan, C.S.1    Ault-Riche, D.B.2    Borchardt, R.T.3
  • 17
    • 0024534958 scopus 로고
    • Rat liver S-adenosylhomocysteinase. Spectrophotometric study of coenzyme binding
    • Gomi, T., Takata, Y., and Fujioka, M. (1989) Rat liver S-adenosylhomocysteinase. Spectrophotometric study of coenzyme binding. Biochim. Biophys. Acta 994, 172-179.
    • (1989) Biochim. Biophys. Acta , vol.994 , pp. 172-179
    • Gomi, T.1    Takata, Y.2    Fujioka, M.3
  • 19
    • 0037172784 scopus 로고    scopus 로고
    • Contributions of active site residues to the partial and overall catalytic activities of human S-adenosylhomocysteine hydrolase
    • Elrod, P., Zhang, J., Yang, X., Yin, D., Hu, Y., Borchardt, R. T., and Schowen, R. L. (2002) Contributions of active site residues to the partial and overall catalytic activities of human S-adenosylhomocysteine hydrolase. Biochemistry 41, 8134-8142.
    • (2002) Biochemistry , vol.41 , pp. 8134-8142
    • Elrod, P.1    Zhang, J.2    Yang, X.3    Yin, D.4    Hu, Y.5    Borchardt, R.T.6    Schowen, R.L.7
  • 20
    • 0031686238 scopus 로고    scopus 로고
    • Helix stabilizing factors and stabilization of thermophilic proteins: An X-ray based study
    • Facchiano, A. M., Colonna, G., and Ragone, R. (1998) Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study. Protein Eng. 11, 753-760.
    • (1998) Protein Eng , vol.11 , pp. 753-760
    • Facchiano, A.M.1    Colonna, G.2    Ragone, R.3
  • 21
    • 0036307678 scopus 로고    scopus 로고
    • Electrostatics significantly affect the stability of designed homeodomain variants
    • Marshall, S. A., Morgan, C. S., and Mayo, S. L. (2002) Electrostatics significantly affect the stability of designed homeodomain variants. J. Mol. Biol. 316, 189-199.
    • (2002) J. Mol. Biol , vol.316 , pp. 189-199
    • Marshall, S.A.1    Morgan, C.S.2    Mayo, S.L.3
  • 22
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • Richardson, J. S., and Richardson, D. C (1988) Amino acid preferences for specific locations at the ends of alpha helices. Science 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.