메뉴 건너뛰기




Volumn 394, Issue 1, 2006, Pages 35-42

Homology-model-guided site-specific mutagenesis reveals the mechanisms of substrate binding and product-regulation of adenosine kinase from Leishmania donovani

Author keywords

Adenosine kinase; AMP regulation; Homology modelling; Leishmania donovani

Indexed keywords

CATALYSIS; HYDROGEN BONDS; MUTAGENESIS; PROTEINS; SUBSTRATES;

EID: 32944465100     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051513     Document Type: Article
Times cited : (6)

References (38)
  • 1
    • 0001653501 scopus 로고
    • The enzymatic synthesis of adenylic acid: Adenosine kinase
    • Caputto, R. (1951) The enzymatic synthesis of adenylic acid: adenosine kinase. J. Biol. Chem. 189, 801-814
    • (1951) J. Biol. Chem. , vol.189 , pp. 801-814
    • Caputto, R.1
  • 2
    • 0001529564 scopus 로고
    • Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside
    • Kornberg, A. and Pricer, Jr, W. E. (1951) Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside. J. Biol. Chem. 193, 481-495
    • (1951) J. Biol. Chem. , vol.193 , pp. 481-495
    • Kornberg, A.1    Pricer Jr., W.E.2
  • 3
    • 0019335866 scopus 로고
    • The stereochemical course of thiophosphoryl group transfer catalyzed by adenosine kinase
    • Richard, J. P., Carr, M. C., Ives, D. H. and Frey, P. A. (1980) The stereochemical course of thiophosphoryl group transfer catalyzed by adenosine kinase. Biochem. Biophys. Res. Commun. 94, 1052-1056
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 1052-1056
    • Richard, J.P.1    Carr, M.C.2    Ives, D.H.3    Frey, P.A.4
  • 4
    • 0030747295 scopus 로고    scopus 로고
    • Hypoxia-induced inhibition of adenosine kinase potentiates cardiac adenosine release
    • Decking, U. K., Schlieper, G., Kroll, K. and Schrader, J. (1997) Hypoxia-induced inhibition of adenosine kinase potentiates cardiac adenosine release. Circ. Res. 2, 154-164
    • (1997) Circ. Res. , vol.2 , pp. 154-164
    • Decking, U.K.1    Schlieper, G.2    Kroll, K.3    Schrader, J.4
  • 6
    • 0020820792 scopus 로고
    • Purine metabolism in Leishmania donovani amastigotes and promastigotes
    • Looker, D. L., Berens, R. L. and Marr, J. J. (1983) Purine metabolism in Leishmania donovani amastigotes and promastigotes. Mol. Biochem. Parasitol. 9, 15-28
    • (1983) Mol. Biochem. Parasitol. , vol.9 , pp. 15-28
    • Looker, D.L.1    Berens, R.L.2    Marr, J.J.3
  • 7
    • 0024337704 scopus 로고
    • The surface membrane 3′-nucleotidase/nuclease of trypanosomatid protozoa
    • Gottlieb, M. (1989) The surface membrane 3′-nucleotidase/nuclease of trypanosomatid protozoa. Parasitol. Today 5, 257-260
    • (1989) Parasitol. Today , vol.5 , pp. 257-260
    • Gottlieb, M.1
  • 8
    • 0023664279 scopus 로고
    • Isolation and characterization of adenosine kinase from Leishmania donovani
    • Datta, A. K., Bhaumik, D. and Chatterjee, R. (1987) Isolation and characterization of adenosine kinase from Leishmania donovani. J. Biol. Chem. 262, 5515-5521
    • (1987) J. Biol. Chem. , vol.262 , pp. 5515-5521
    • Datta, A.K.1    Bhaumik, D.2    Chatterjee, R.3
  • 9
    • 0023921092 scopus 로고
    • Reaction kinetics and inhibition of adenosine kinase from Leishmania donovani
    • Bhaumik, D. and Datta, A. K. (1988) Reaction kinetics and inhibition of adenosine kinase from Leishmania donovani. Mol. Biochem. Parasitol. 28, 181-187
    • (1988) Mol. Biochem. Parasitol. , vol.28 , pp. 181-187
    • Bhaumik, D.1    Datta, A.K.2
  • 10
    • 0024515643 scopus 로고
    • Immunochemical and catalytic characteristics of adenosine kinase from Leishmania donovani
    • Bhaumik, D. and Datta, A. K. (1989) Immunochemical and catalytic characteristics of adenosine kinase from Leishmania donovani. J. Biol. Chem. 264, 4356-4361
    • (1989) J. Biol. Chem. , vol.264 , pp. 4356-4361
    • Bhaumik, D.1    Datta, A.K.2
  • 11
    • 0026519037 scopus 로고
    • Active site thiol(s) in Leishmania donovani adenosine kinase: Comparison with hamster enzyme and evidence for the absence of regulatory adenosine binding site
    • Bhaumik, D. and Dalta, A. K. (1992) Active site thiol(s) in Leishmania donovani adenosine kinase: comparison with hamster enzyme and evidence for the absence of regulatory adenosine binding site. Mol. Biochem. Parasitol. 52, 29-38
    • (1992) Mol. Biochem. Parasitol. , vol.52 , pp. 29-38
    • Bhaumik, D.1    Dalta, A.K.2
  • 12
    • 0028261926 scopus 로고
    • Probing the function(s) of active-site arginine residue in Leishmania donovani adenosine kinase
    • Ghosh, M. and Datta, A. K. (1994) Probing the function(s) of active-site arginine residue in Leishmania donovani adenosine kinase. Biochem. J. 298, 295-301
    • (1994) Biochem. J. , vol.298 , pp. 295-301
    • Ghosh, M.1    Datta, A.K.2
  • 13
    • 0029954419 scopus 로고    scopus 로고
    • Two conformationally vicinal thiols at the active site of Leishmania donovani adenosine kinase
    • Bagui, T. K., Ghosh, M. and Datta, A. K. (1996) Two conformationally vicinal thiols at the active site of Leishmania donovani adenosine kinase. Biochem. J. 316, 439-445
    • (1996) Biochem. J. , vol.316 , pp. 439-445
    • Bagui, T.K.1    Ghosh, M.2    Datta, A.K.3
  • 14
    • 0033136251 scopus 로고    scopus 로고
    • Molecular cloning and expression of adenosine kinase from Leishmania donovani: Identification of unconventional P-loop motif
    • Sinha, K. M., Ghosh, M., Das, I. and Datta, A. K. (1999) Molecular cloning and expression of adenosine kinase from Leishmania donovani: identification of unconventional P-loop motif. Biochem. J. 339, 667-673
    • (1999) Biochem. J. , vol.339 , pp. 667-673
    • Sinha, K.M.1    Ghosh, M.2    Das, I.3    Datta, A.K.4
  • 15
    • 0025828793 scopus 로고
    • Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: Evidence for a kinase superfamily including both phosphofructokinases of Escherichia coll
    • Wu, L. F., Reizer, A., Reizer, J., Cai, B., Tomich, J. M. and Saier, Jr, M. H. (1991) Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: evidence for a kinase superfamily including both phosphofructokinases of Escherichia coll. J. Bacteriol. 173, 3117-3127
    • (1991) J. Bacteriol. , vol.173 , pp. 3117-3127
    • Wu, L.F.1    Reizer, A.2    Reizer, J.3    Cai, B.4    Tomich, J.M.5    Saier Jr., M.H.6
  • 16
    • 0027404023 scopus 로고
    • Convergent evolution of similar enzymatic function on different protein folds: The hexokinase, ribokinase, and galactokinase families of sugar kinases
    • Bork, P., Sander, C. and Valencia, A. (1993) Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci. 2, 31-40
    • (1993) Protein Sci. , vol.2 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 17
    • 0032506161 scopus 로고    scopus 로고
    • Structure of human adenosine kinase at 1.5 Å resolution
    • Mathews, I. I., Erion, M. D. and Ealick, S. E. (1998) Structure of human adenosine kinase at 1.5 Å resolution. Biochemistry. 37, 15607-15620
    • (1998) Biochemistry , vol.37 , pp. 15607-15620
    • Mathews, I.I.1    Erion, M.D.2    Ealick, S.E.3
  • 18
    • 0034685603 scopus 로고    scopus 로고
    • Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding
    • Schumacher, M. A., Scott, D. M., Mathews, I. I., Ealick, S. E., Roos, D. S., Ullman, B. and Brennan, R. G. (2000) Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding. J. Mol. Biol. 298, 875-893
    • (2000) J. Mol. Biol. , vol.298 , pp. 875-893
    • Schumacher, M.A.1    Scott, D.M.2    Mathews, I.I.3    Ealick, S.E.4    Roos, D.S.5    Ullman, B.6    Brennan, R.G.7
  • 19
    • 18844452613 scopus 로고    scopus 로고
    • Mutational analysis of the active-site residues crucial for catalytic activity of adenosine kinase from Leishmania donovani
    • Datta, R., Das, I., Sen, B., Chakraborty, A., Adak, S., Mandal, C. and Datta, A. K. (2005) Mutational analysis of the active-site residues crucial for catalytic activity of adenosine kinase from Leishmania donovani. Biochem. J. 387, 591-600
    • (2005) Biochem. J. , vol.387 , pp. 591-600
    • Datta, R.1    Das, I.2    Sen, B.3    Chakraborty, A.4    Adak, S.5    Mandal, C.6    Datta, A.K.7
  • 20
    • 0019321165 scopus 로고
    • Human placental adenosine kinase: Kinetic mechanism and inhibition
    • Palella, T. D., Andres, C. M. and Fox, I. H. (1980) Human placental adenosine kinase: kinetic mechanism and inhibition. J. Biol. Chem. 255, 5264-5269
    • (1980) J. Biol. Chem. , vol.255 , pp. 5264-5269
    • Palella, T.D.1    Andres, C.M.2    Fox, I.H.3
  • 21
    • 0023220786 scopus 로고
    • Adenosine kinase from human erythrocytes: Kinetic studies and characterization of adenosine binding sites
    • Hawkins, C. F. and Bagnara, A. S. (1987) Adenosine kinase from human erythrocytes: kinetic studies and characterization of adenosine binding sites. Biochemistry 26, 1982-1987
    • (1987) Biochemistry , vol.26 , pp. 1982-1987
    • Hawkins, C.F.1    Bagnara, A.S.2
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0013612812 scopus 로고
    • (Boyer, P. D., ed.), 3rd edn, Academic Press, New York
    • Cleland, W. W. (1970) The Enzymes (Boyer, P. D., ed.), 3rd edn, vol. 2, pp. 1-65, Academic Press, New York
    • (1970) The Enzymes , vol.2 , pp. 1-65
    • Cleland, W.W.1
  • 24
    • 0021107943 scopus 로고
    • Site-directed mutagenesis as a probe of enzyme structure and catalysis: Tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation
    • Wilkinson, A. J., Fersht, A. R., Blow, D. M. and Winter, G. (1983) Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation. Biochemistry 22, 3581-3586
    • (1983) Biochemistry , vol.22 , pp. 3581-3586
    • Wilkinson, A.J.1    Fersht, A.R.2    Blow, D.M.3    Winter, G.4
  • 25
    • 0022996027 scopus 로고
    • Hydrogen bonding and specificity: Fluorodeoxy sugars as probes of hydrogen bonding in the glycogen phosphorylase-glucose complex
    • Street, I. P., Armstrong, C. R. and Withers, S. G. (1986) Hydrogen bonding and specificity: fluorodeoxy sugars as probes of hydrogen bonding in the glycogen phosphorylase-glucose complex. Biochemistry 25, 6021-6027
    • (1986) Biochemistry , vol.25 , pp. 6021-6027
    • Street, I.P.1    Armstrong, C.R.2    Withers, S.G.3
  • 26
    • 0026515012 scopus 로고
    • Kinetic identification of a hydrogen bonding pair in the glucoamylase-maltose transition state complex
    • Sierks, M. R. and Svensson, B. (1992) Kinetic identification of a hydrogen bonding pair in the glucoamylase-maltose transition state complex. Protein Eng. 5, 185-188
    • (1992) Protein Eng. , vol.5 , pp. 185-188
    • Sierks, M.R.1    Svensson, B.2
  • 27
    • 32944470614 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 28
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 29
    • 0032520213 scopus 로고    scopus 로고
    • Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 Å resolution: Insights into a new family of kinase structures
    • Sigrell, J. A., Cameron, A. D., Jones, T. A. and Mowbray, S. L. (1998) Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 Å resolution: insights into a new family of kinase structures. Structure 6, 183-193
    • (1998) Structure , vol.6 , pp. 183-193
    • Sigrell, J.A.1    Cameron, A.D.2    Jones, T.A.3    Mowbray, S.L.4
  • 30
    • 0022378459 scopus 로고
    • Regulation of deoxyadenosine and nucleoside analog phosphorylation by human placental adenosine kinase
    • Hurley, M. C., Lin, B. and Fox, I. H. (1985) Regulation of deoxyadenosine and nucleoside analog phosphorylation by human placental adenosine kinase. J. Biol. Chem. 260, 15675-15681
    • (1985) J. Biol. Chem. , vol.260 , pp. 15675-15681
    • Hurley, M.C.1    Lin, B.2    Fox, I.H.3
  • 32
    • 0029066380 scopus 로고
    • Structure-activity relationship for the binding of nucleoside ligands to adenosine kinase from Toxoplasma gondii
    • Iltzsch, M. H., Uber, S. S., Tankersley, K. O. and el Kouni, M. H. (1995) Structure-activity relationship for the binding of nucleoside ligands to adenosine kinase from Toxoplasma gondii. Biochem. Pharmacol. 49, 1501-1512
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 1501-1512
    • Iltzsch, M.H.1    Uber, S.S.2    Tankersley, K.O.3    El Kouni, M.H.4
  • 33
    • 1342310509 scopus 로고    scopus 로고
    • Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase
    • Rothman, S. C., Voorhies, M. and Kirsch, J. F. (2004) Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase. Protein Sci. 3, 763-772
    • (2004) Protein Sci. , vol.3 , pp. 763-772
    • Rothman, S.C.1    Voorhies, M.2    Kirsch, J.F.3
  • 34
    • 0033578713 scopus 로고    scopus 로고
    • Tryptophan 409 controls the activity of neuronal nitric-oxide synthase by regulating nitric oxide feedback inhibition
    • Adak, S., Crooks, C., Wang, Q., Crane, B. R., Tainer, J. A., Getzoff, E. D. and Stuehr, D. J. (1999) Tryptophan 409 controls the activity of neuronal nitric-oxide synthase by regulating nitric oxide feedback inhibition. J. Biol. Chem. 274, 26907-26911
    • (1999) J. Biol. Chem. , vol.274 , pp. 26907-26911
    • Adak, S.1    Crooks, C.2    Wang, Q.3    Crane, B.R.4    Tainer, J.A.5    Getzoff, E.D.6    Stuehr, D.J.7
  • 35
    • 0021907722 scopus 로고
    • Leishmania mexicana: Purine-metabolizing enzymes of amastigotes and promastigotes
    • Hassan, H. F. and Coombs, G. H. (1985) Leishmania mexicana: purine-metabolizing enzymes of amastigotes and promastigotes. Exp. Parasitol. 59, 139-150
    • (1985) Exp. Parasitol. , vol.59 , pp. 139-150
    • Hassan, H.F.1    Coombs, G.H.2
  • 36
    • 0033618324 scopus 로고    scopus 로고
    • Induced fit on sugar binding activates ribokinase
    • Sigrell, J. A., Cameron, A. D. and Mowbray, S. L. (1999) Induced fit on sugar binding activates ribokinase. J. Mol. Biol. 290, 1009-1018
    • (1999) J. Mol. Biol. , vol.290 , pp. 1009-1018
    • Sigrell, J.A.1    Cameron, A.D.2    Mowbray, S.L.3
  • 37
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • Volkman, B. F., Lipson, D., Wemmer, D. E. and Kern, D. (2001) Two-state allosteric behavior in a single-domain signaling protein. Science 291, 2429-2433
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 38
    • 4043052955 scopus 로고    scopus 로고
    • NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: Implications for the allosteric mechanism
    • Revington, M., Holder, T. M. and Zuiderweg, E. R. (2004) NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism. J. Biol. Chem. 279, 33958-33967
    • (2004) J. Biol. Chem. , vol.279 , pp. 33958-33967
    • Revington, M.1    Holder, T.M.2    Zuiderweg, E.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.