메뉴 건너뛰기




Volumn 17, Issue 2, 2010, Pages 197-205

Kinetic and conformational studies of adenosine deaminase upon interaction with oxazepam and lorazepam

Author keywords

Adenosine deaminase; Kinetics; Lorazepam; Oxazepam; Structures

Indexed keywords

ADENOSINE; ADENOSINE DEAMINASE; ANTICONVULSIVE AGENT; ANXIOLYTIC AGENT; ENZYME INHIBITOR; HYPNOTIC SEDATIVE AGENT; LIGAND; LORAZEPAM; OXAZEPAM;

EID: 77949956630     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986610790226076     Document Type: Article
Times cited : (1)

References (31)
  • 1
    • 0019108091 scopus 로고
    • In Isoenzymes of adenosine deaminase
    • Rattazzi M.C.; Scandalios J.G.; Whitt G.S. Eds., Alan RLiss: New York
    • Hirshhorn, R.; Ratech, H.; In Isoenzymes of adenosine deaminase. In Isoenzymes: Current Topics in Biological and Medical Research, Rattazzi M.C.; Scandalios J.G.; Whitt G.S. Eds., Alan RLiss: New York, 1980; Vol. 4, pp. 131-157.
    • (1980) In Isoenzymes: Current Topics In Biological and Medical Research , vol.4 , pp. 131-157
    • Hirshhorn, R.1    Ratech, H.2
  • 2
    • 0026434561 scopus 로고
    • Atomic structure of adenosine deaminase complexed with a transition-state analog: Understanding catalysis and immunodeficiency mutations
    • Wilson, D.K.; Rudolph, F.B.; Quiocho F.A. Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations. Science,1991, 252(5010), 1278-1284.
    • (1991) Science , vol.252 , Issue.5010 , pp. 1278-1284
    • Wilson, D.K.1    Rudolph, F.B.2    Quiocho, F.A.3
  • 3
    • 0030045246 scopus 로고    scopus 로고
    • Characterization of adenosinedeaminase binding to human CD26 on T cells and its biologic rolein immune response
    • Dong, R.P.; Kameoka, J.; Hegen, M.; Tanaka, T.; Xu, T.H.; Schlossman, S.F.; Morimoto, C. Characterization of adenosinedeaminase binding to human CD26 on T cells and its biologic rolein immune response. J. Immunol., 1996, 156(4), 1349-1355.
    • (1996) J. Immunol , vol.156 , Issue.4 , pp. 1349-1355
    • Dong, R.P.1    Kameoka, J.2    Hegen, M.3    Tanaka, T.4    Xu, T.H.5    Schlossman, S.F.6    Morimoto, C.7
  • 5
    • 0031723552 scopus 로고    scopus 로고
    • Adenosine deaminase deficiency: Clinical expression, molecular basis and therapy
    • Hershfield, M.S. Adenosine deaminase deficiency: clinical expression, molecular basis and therapy. Semin. Hematol., 1998, 35(4),291-298.
    • (1998) Semin. Hematol , vol.35 , Issue.4 , pp. 291-298
    • Hershfield, M.S.1
  • 7
    • 0023181468 scopus 로고
    • Genetic expression ofadenosine deaminase in human lymphoid malignancies
    • Gan, T.E.; Dadonna, P.E.; Mitchell, B.S. Genetic expression ofadenosine deaminase in human lymphoid malignancies. Blood,1987, 69 (5), 1376-1380.
    • (1987) Blood , vol.69 , Issue.5 , pp. 1376-1380
    • Gan, T.E.1    Dadonna, P.E.2    Mitchell, B.S.3
  • 8
    • 0026078718 scopus 로고
    • Develop-mental expression of adenosine deaminase during decidualizationin the rat uterus
    • Hong, L.; Mulholland, J.; Chinsky, J.M.; Knudsen, T.B. Develop-mental expression of adenosine deaminase during decidualizationin the rat uterus. Biol. Repord., 1991, 44(1), 83-93.
    • (1991) Biol. Repord , vol.44 , Issue.1 , pp. 83-93
    • Hong, L.1    Mulholland, J.2    Chinsky, J.M.3    Knudsen, T.B.4
  • 9
    • 0019837565 scopus 로고
    • The role of adenosine and its nucleotides incentral synaptic transmission
    • Phillis, J.W.; Wu, P.H. The role of adenosine and its nucleotides incentral synaptic transmission. Prog. Neurobiol., 1981, 16(3-4),187-239.
    • (1981) Prog. Neurobiol , vol.16 , Issue.3-4 , pp. 187-239
    • Phillis, J.W.1    Wu, P.H.2
  • 11
    • 0028905177 scopus 로고
    • Lipophilic, acid-stable, adenosinedeaminase-activated anti-HIV prodrugs for central nervous systemdelivery. 2. 6-Halo and 6-alkoxy prodrugs of 2'-beta-fluoro-2',3'-dideoxyinosine
    • Ford, H.; Siddiqui, M.A.; Driscoll, J.S.; Marquez, V.E.; Kelly J.A.; Mitsuya, H.; Shirasaka, T. Lipophilic, acid-stable, adenosinedeaminase-activated anti-HIV prodrugs for central nervous systemdelivery. 2. 6-Halo and 6-alkoxy prodrugs of 2'-beta-fluoro-2',3'-dideoxyinosine. J. Med. Chem., 1995, 38(7), 1189-1195.
    • (1995) J. Med. Chem , vol.38 , Issue.7 , pp. 1189-1195
    • Ford, H.1    Siddiqui, M.A.2    Driscoll, J.S.3    Marquez, V.E.4    Kelly, J.A.5    Mitsuya, H.6    Shirasaka, T.7
  • 12
    • 0021216952 scopus 로고
    • Human adenosine deaminase. cDNA and complete primary amino acid sequence
    • Doddona, P.E.; Schewach, D.S.; Kelly, W.N.; Argos, P.; Markham, A.F.; Orkin, S.H. Human adenosine deaminase. cDNA and complete primary amino acid sequence. Biol. Chem., 1984, 259(19),12101-12106.
    • (1984) Biol. Chem , vol.259 , Issue.19 , pp. 12101-12106
    • Doddona, P.E.1    Schewach, D.S.2    Kelly, W.N.3    Argos, P.4    Markham, A.F.5    Orkin, S.H.6
  • 13
    • 0026018939 scopus 로고
    • Deducedamino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: Implicationsfor catalytic function
    • Chang, Z.; Nygaard, P.; Chinualt, A.C.; Kellems, R.E. Deducedamino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implicationsfor catalytic function. Biochemistry, 1991, 30(8), 2275-2280.
    • (1991) Biochemistry , vol.30 , Issue.8 , pp. 2275-2280
    • Chang, Z.1    Nygaard, P.2    Chinualt, A.C.3    Kellems, R.E.4
  • 14
    • 0027398949 scopus 로고
    • A pre-transition-state mimic of anenzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water
    • Wilson, D.K.; Quiocho, F.A. A pre-transition-state mimic of anenzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water. Biochemistry, 1993,32(7), 1689-1694.
    • (1993) Biochemistry , vol.32 , Issue.7 , pp. 1689-1694
    • Wilson, D.K.1    Quiocho, F.A.2
  • 16
    • 0027456581 scopus 로고
    • Mutationalanalysis of active site residues of human adenosine deaminase
    • Bhaumik, D.; Medin, J.; Gathy, K.; Coleman, M.S. Mutationalanalysis of active site residues of human adenosine deaminase. J.Biol. Chem., 1993, 268(8), 5464-5470.
    • (1993) J. Biol. Chem , vol.268 , Issue.8 , pp. 5464-5470
    • Bhaumik, D.1    Medin, J.2    Gathy, K.3    Coleman, M.S.4
  • 17
    • 40949109275 scopus 로고    scopus 로고
    • A study on the inhibition of adenosine deaminase
    • Alunni, S.; Orru, M.; Ottavi, L. A study on the inhibition of adenosine deaminase. J. Enzyme. Inhib. Med. Chem., 2008, 23(2), 182-189.
    • (2008) J. Enzyme. Inhib. Med. Chem , vol.23 , Issue.2 , pp. 182-189
    • Alunni, S.1    Orru, M.2    Ottavi, L.3
  • 19
    • 0021986937 scopus 로고
    • Trazodone a nontricyclic antidepressant, is an inhibitor of adenosine deaminase
    • Sheid, B. Trazodone a nontricyclic antidepressant, is an inhibitor of adenosine deaminase. Res. Commun. Chem. Pathol. Pharmacol.,1985, 47(1), 149-152.
    • (1985) Res. Commun. Chem. Pathol. Pharmacol , vol.47 , Issue.1 , pp. 149-152
    • Sheid, B.1
  • 20
    • 0000267781 scopus 로고
    • Specific adenosine deaminase from intestine
    • Kaplan, N.O. Specific adenosine deaminase from intestine. Methods Enzymol., 1955; Vol. 2, 473-475.
    • (1955) Methods Enzymol , vol.2 , pp. 473-475
    • Kaplan, N.O.1
  • 21
    • 38049159940 scopus 로고    scopus 로고
    • Activity of adenosine deaminase and adenylate deaminase on adenosineand 2', 3'-isopropylidene adenosine: Role of the protecting group atdifferent pH values
    • Alessandrini, L.; Ciuffreda, P.; Pavlovic, R.; Santaniello, E. Activity of adenosine deaminase and adenylate deaminase on adenosineand 2', 3'-isopropylidene adenosine: Role of the protecting group atdifferent pH values. Nucleosides Nucleotides Nucleic Acids, 2008,27(1), 31-36.
    • (2008) Nucleosides Nucleotides Nucleic Acids , vol.27 , Issue.1 , pp. 31-36
    • Alessandrini, L.1    Ciuffreda, P.2    Pavlovic, R.3    Santaniello, E.4
  • 22
    • 0022503457 scopus 로고
    • Calculation of proteinconformation from circular dichroism
    • Yang, J.T.; Wu, C.S.C.; Martinez, H.M. Calculation of proteinconformation from circular dichroism. Methods Enzymol., 1986,Vol. 130, 208-269.
    • (1986) Methods Enzymol , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.C.2    Martinez, H.M.3
  • 23
    • 0020184861 scopus 로고
    • Experimental errors andtheir effect on analyzing circular dichroism spectra of proteins
    • Hennessey, J.P., Jr; Johnson, W.C., Jr. Experimental errors andtheir effect on analyzing circular dichroism spectra of proteins. Anal. Biochem., 1982, 125(1), 177-188.
    • (1982) Anal. Biochem , vol.125 , Issue.1 , pp. 177-188
    • Hennessey Jr., J.P.1    Johnson Jr., W.C.2
  • 26
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G.M.; Goodsell, D.S.; Halliday, R.S.; Huey, R.; Hart, W.E.; Belew, R.K.; Olson, A.J. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem., 1998, 19(14), 1639-1662.
    • (1998) J. Comput. Chem , vol.19 , Issue.14 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 28
    • 0034661399 scopus 로고    scopus 로고
    • Noncompetitive, reversible inhibition of aminoacylase-1 by a series of L-alpha-hydroxyl and L-alpha-fluoro fatty acids: Ligand specificity of aspergillus oryzae andporcine kidney enzymes
    • Tamura, T.; Oki, Y.; Yoshida, A.; Kuriyama, T.; Kawakami, H.; Inoue, H.; Inagaki, K.; Tanaka, H. Noncompetitive, reversible inhibition of aminoacylase-1 by a series of L-alpha-hydroxyl and L-alpha-fluoro fatty acids: ligand specificity of aspergillus oryzae andporcine kidney enzymes. Arch. Biochem. Biophys., 2000, 379(2),261-266.
    • (2000) Arch. Biochem. Biophys , vol.379 , Issue.2 , pp. 261-266
    • Tamura, T.1    Oki, Y.2    Yoshida, A.3    Kuriyama, T.4    Kawakami, H.5    Inoue, H.6    Inagaki, K.7    Tanaka, H.8
  • 29
    • 0035903877 scopus 로고    scopus 로고
    • Hydro-phobicity, a physicochemical factor in the inhibition of the enzymeestrone sulfatase
    • Ahmed, S.; James, K.; Owen, C.P.; Patel, C.K.; Patel, M. Hydro-phobicity, a physicochemical factor in the inhibition of the enzymeestrone sulfatase. Bioorg. Med. Chem. Lett., 2001, 11(18), 2525-2528.
    • (2001) Bioorg. Med. Chem. Lett , vol.11 , Issue.18 , pp. 2525-2528
    • Ahmed, S.1    James, K.2    Owen, C.P.3    Patel, C.K.4    Patel, M.5
  • 30
    • 0031907425 scopus 로고    scopus 로고
    • Guidelines for the interpretation of analytical toxicology results and unit of measurement conversion factors
    • Flanagan, R.J. Guidelines for the interpretation of analytical toxicology results and unit of measurement conversion factors. Ann. Clin. Biochem., 1998, 35(Pt 2), 261-267.
    • (1998) Ann. Clin. Biochem , vol.35 , Issue.PART 2 , pp. 261-267
    • Flanagan, R.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.