메뉴 건너뛰기




Volumn 23, Issue 2, 2008, Pages 182-189

A study on the inhibition of adenosine deaminase

Author keywords

Adenosine deaminase; Inhibition; Kinetics; Mechanism

Indexed keywords

2 AMINOPURINE; 4 AMINOPYRIDINE; 4 AMINOPYRIMIDINE; 4 HYDROXYPYRIDINE; ADENINE; ADENOSINE DEAMINASE; ENZYME INHIBITOR; INOSINE; PHENYLHYDRAZINE; PURINE; UNCLASSIFIED DRUG;

EID: 40949109275     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.1080/14756360701475233     Document Type: Article
Times cited : (19)

References (47)
  • 2
  • 3
    • 0017565851 scopus 로고
    • Purification and properties of the adenosine deaminase from the midgut gland of a marine bivalved mollusc
    • Aikawa, T., Umemori-Aikawa, Y. and Fisher, JR (1977) Purification and properties of the adenosine deaminase from the midgut gland of a marine bivalved mollusc. Atrina spp Comp Biochem Physiol, 58, pp. 357-364.
    • (1977) Atrina Spp Comp Biochem Physiol , vol.58 , pp. 357-364
    • Aikawa, T.1    Umemori-Aikawa, Y.2    Fisher, J.R.3
  • 4
    • 0014428399 scopus 로고
    • Two different hepatic adenosine deaminase in the chicken
    • Ma, PF and Fisher, JR (1968) Two different hepatic adenosine deaminase in the chicken. Biochim Biophys Acta, 159, pp. 153-159.
    • (1968) Biochim Biophys Acta , vol.159 , pp. 153-159
    • Ma, P.F.1    Fisher, J.R.2
  • 5
    • 50549198581 scopus 로고
    • Tissue distribution of adenosine deaminase in six mammal species
    • Brady, TG and O'Donovan, CI (1965) Tissue distribution of adenosine deaminase in six mammal species. Comp Biochem Physiol, 14, pp. 101-119.
    • (1965) Comp Biochem Physiol , vol.14 , pp. 101-119
    • Brady, T.G.1    O'Donovan, C.I.2
  • 6
    • 0026562988 scopus 로고
    • Adenosine deaminase from bovine brain: Purification and partial characterization
    • Lupidi, G., Marmocchi, F., Falasca, M., Venardi, G., Cristalli, G. and Riva, F. (1992) Adenosine deaminase from bovine brain: Purification and partial characterization. Biochem Int, 26, pp. 1053-1063.
    • (1992) Biochem Int , vol.26 , pp. 1053-1063
    • Lupidi, G.1    Marmocchi, F.2    Falasca, M.3    Venardi, G.4    Cristalli, G.5    Riva, F.6
  • 7
    • 0016852319 scopus 로고
    • Adenosine deaminase from human erythrocytes: Purification and effects of adenosine analogs
    • Argwal, RP, Sagar, SM and Parks Jr, RE (1975) Adenosine deaminase from human erythrocytes: Purification and effects of adenosine analogs. Biochem Pharmacol, 24, pp. 693-701.
    • (1975) Biochem Pharmacol , vol.24 , pp. 693-701
    • Argwal, R.P.1    Sagar, S.M.2    Parks Jr., R.E.3
  • 8
    • 0017335695 scopus 로고
    • Analysis of normal and mutants forms of human adenosine deaminase
    • Daddona, PE and Kelly, WN (1980) Analysis of normal and mutants forms of human adenosine deaminase. J Biol Chem, 252, pp. 110-115.
    • (1980) J Biol Chem , vol.252 , pp. 110-115
    • Daddona, P.E.1    Kelly, W.N.2
  • 9
    • 0019877829 scopus 로고
    • Human adenosine deaminase: Properties and turnover in cultured T and B lymphoblast
    • Daddona, PE (1981) Human adenosine deaminase: Properties and turnover in cultured T and B lymphoblast. J Biol Chem, 256, pp. 12496-12501.
    • (1981) J Biol Chem , vol.256 , pp. 12496-12501
    • Daddona, P.E.1
  • 11
    • 0033397311 scopus 로고    scopus 로고
    • Crystallization and preliminary analysis of bovine adenosine deaminase
    • Kinoshita, T., Nishio, N., Sato, A. and Murata, M. (1999) Crystallization and preliminary analysis of bovine adenosine deaminase. Acta Crystallogr, pp. 2031-2032.
    • (1999) Acta Crystallogr , pp. 2031-2032
    • Kinoshita, T.1    Nishio, N.2    Sato, A.3    Murata, M.4
  • 12
    • 0142187618 scopus 로고    scopus 로고
    • The mechanism of adenosine deaminase catalysis studied by QM/MM calculations: The role of histidine 238 and the activity of the alanine 238
    • Gleeson, MP, Burton, NA and Hillier, IH (2003) The mechanism of adenosine deaminase catalysis studied by QM/MM calculations: The role of histidine 238 and the activity of the alanine 238. Phys Chem Chem Phys, 5, pp. 4272-4278.
    • (2003) Phys Chem Chem Phys , vol.5 , pp. 4272-4278
    • Gleeson, M.P.1    Burton, N.A.2    Hillier, I.H.3
  • 13
    • 0017278672 scopus 로고
    • Enhancement of 9-beta-d-arabinofuranosyladenine cytotoxicity to mouse leukemia L1210 in vitro by 2′-deoxycoformycin
    • Cass, CE and Au-Yeung, TH (1976) Enhancement of 9-beta-d-arabinofuranosyladenine cytotoxicity to mouse leukemia L1210 in vitro by 2′-deoxycoformycin. Cancer Res, 36, pp. 1486-1491.
    • (1976) Cancer Res , vol.36 , pp. 1486-1491
    • Cass, C.E.1    Au-Yeung, T.H.2
  • 14
    • 0017155480 scopus 로고
    • Enhancement of the biological activity of cordycepin(3′-deoxyadenosine) by the adenosine inhibitor 2′-deoxycoformycin
    • Johns, DG and Adamson, RH (1976) Enhancement of the biological activity of cordycepin(3′-deoxyadenosine) by the adenosine inhibitor 2′-deoxycoformycin. Biochem Pharmacol, 25, pp. 1441-1444.
    • (1976) Biochem Pharmacol , vol.25 , pp. 1441-1444
    • Johns, D.G.1    Adamson, R.H.2
  • 15
    • 0017282589 scopus 로고
    • Enhancement of the antitumor activity of arabinofuranosyladenine by 2′-deoxycoformicin
    • LePage, GA, Worth, IS and Kimball, AP (1976) Enhancement of the antitumor activity of arabinofuranosyladenine by 2′-deoxycoformicin. Cancer Res, 36, pp. 1481-1485.
    • (1976) Cancer Res , vol.36 , pp. 1481-1485
    • LePage, G.A.1    Worth, I.S.2    Kimball, A.P.3
  • 16
    • 0017616970 scopus 로고
    • Enhancement of the biological activity of adenosine analogs by the adenosine deaminase inhibitor 2′-deoxycoformycin
    • Adamson, RH, Zaharevitz, DW and Johns, DG (1977) Enhancement of the biological activity of adenosine analogs by the adenosine deaminase inhibitor 2′-deoxycoformycin. Pharmacology, 15, pp. 84-89.
    • (1977) Pharmacology , vol.15 , pp. 84-89
    • Adamson, R.H.1    Zaharevitz, D.W.2    Johns, D.G.3
  • 17
    • 0018104546 scopus 로고
    • Potentiation by 2′-deoxycoformycin of the inhibitory effect by 3′-deoxyadenosine(cordycepin) on nuclear RNA synthesis in L210 cells in vitro
    • Glazer, RI, Lott, TJ and Peale, AL (1978) Potentiation by 2′-deoxycoformycin of the inhibitory effect by 3′-deoxyadenosine(cordycepin) on nuclear RNA synthesis in L210 cells in vitro. Cancer Res, 38, pp. 2233-2238.
    • (1978) Cancer Res , vol.38 , pp. 2233-2238
    • Glazer, R.I.1    Lott, T.J.2    Peale, A.L.3
  • 18
    • 0021996477 scopus 로고
    • Effects of adenosine deaminase inhibitor 2′-deoxycoformycin on the repair and expression of potentially lethal damage sensitive to β-araA
    • Iliakis, G. and Ngo, FQH (1985) Effects of adenosine deaminase inhibitor 2′-deoxycoformycin on the repair and expression of potentially lethal damage sensitive to β-araA. Radiat Environ Biophys, 24, pp. 81-88.
    • (1985) Radiat Environ Biophys , vol.24 , pp. 81-88
    • Iliakis, G.1    Ngo, F.Q.H.2
  • 19
    • 0027526551 scopus 로고
    • Increases in interstitial adenosine and cerebral blood flow with inhibition of adenosine kinase and adenosine deaminase
    • Sciotti, VM and Van Wylen, DGL (1993) Increases in interstitial adenosine and cerebral blood flow with inhibition of adenosine kinase and adenosine deaminase. J Cerebral Blood Flow Metab, 13, pp. 201-207.
    • (1993) J Cerebral Blood Flow Metab , vol.13 , pp. 201-207
    • Sciotti, V.M.1    Van Wylen, D.G.L.2
  • 20
    • 0029057439 scopus 로고
    • Involvement of adenosine deaminase and adenosine kinase in regulating extracellular adenosine concentration in rat hippocampal slices
    • Llyod, HGE and Fredholm, BB (1995) Involvement of adenosine deaminase and adenosine kinase in regulating extracellular adenosine concentration in rat hippocampal slices. Neurochem Int, 26, pp. 387-395.
    • (1995) Neurochem Int , vol.26 , pp. 387-395
    • Llyod, H.G.E.1    Fredholm, B.B.2
  • 21
    • 0028823743 scopus 로고
    • Modulation of adenosine release from rat spinal cord by adenosine deaminase and adenosine kinase inhibitors
    • Golembiowska, K., White, TD and Sawynok, J. (1995) Modulation of adenosine release from rat spinal cord by adenosine deaminase and adenosine kinase inhibitors. Brain Res, 699, pp. 315-320.
    • (1995) Brain Res , vol.699 , pp. 315-320
    • Golembiowska, K.1    White, T.D.2    Sawynok, J.3
  • 22
    • 0006028835 scopus 로고
    • Pharmacological augmentation of excitatory amino acid-evoked adenosine release from rat cortical slices
    • White, TD (1994) Pharmacological augmentation of excitatory amino acid-evoked adenosine release from rat cortical slices. Drug Dev Res, 31, p. 333.
    • (1994) Drug Dev Res , vol.31 , pp. 333
    • White, T.D.1
  • 23
    • 0029996021 scopus 로고    scopus 로고
    • Potentation of excitatory amino acid-evoked adenosine release from rat cortex by inhibitors of adenosine kinase and adenosine deaminase and by acadesine
    • White, TD (1996) Potentation of excitatory amino acid-evoked adenosine release from rat cortex by inhibitors of adenosine kinase and adenosine deaminase and by acadesine. Eur J Pharmacol, 303, pp. 27-38.
    • (1996) Eur J Pharmacol , vol.303 , pp. 27-38
    • White, T.D.1
  • 24
    • 0032485398 scopus 로고    scopus 로고
    • Co-administration of adenosine kinase and deaminase inhibitors produces supra-additive potentiation of N-methyl-D-aspartate-evoked adenosine formation in cortex
    • Hebb, MO and White, TD (1998) Co-administration of adenosine kinase and deaminase inhibitors produces supra-additive potentiation of N-methyl-D-aspartate-evoked adenosine formation in cortex. Eur J Pharmacol, 344, pp. 121-125.
    • (1998) Eur J Pharmacol , vol.344 , pp. 121-125
    • Hebb, M.O.1    White, T.D.2
  • 25
    • 0033458946 scopus 로고    scopus 로고
    • Antinociceptive and anti-inflammatory properties of an adenosine kinase inhibitor and an adenosine deaminase inhibitor
    • Poon, A. and Saynok, J. (1999) Antinociceptive and anti-inflammatory properties of an adenosine kinase inhibitor and an adenosine deaminase inhibitor. Eur J Pharmacol, 384, pp. 123-138.
    • (1999) Eur J Pharmacol , vol.384 , pp. 123-138
    • Poon, A.1    Saynok, J.2
  • 26
    • 0031922416 scopus 로고    scopus 로고
    • Effects of adenosine deaminase inhibition on blood pressure in old spontaneously hypertensive rats
    • Tofovic, SP, Kusaka, H., Li, P. and Jackson, EK (1998) Effects of adenosine deaminase inhibition on blood pressure in old spontaneously hypertensive rats. Clin Exp Hyperten, 20, pp. 329-344.
    • (1998) Clin Exp Hyperten , vol.20 , pp. 329-344
    • Tofovic, S.P.1    Kusaka, H.2    Li, P.3    Jackson, E.K.4
  • 27
    • 0028843617 scopus 로고
    • The role of dehydroalanine in catalysis by histidine ammonia lyase
    • Langer, M., Pauling, A. and Rétey, J. (1995) The role of dehydroalanine in catalysis by histidine ammonia lyase. Angew Chem Int Ed Engl, 34, pp. 1464-1465.
    • (1995) Angew Chem Int Ed Engl , vol.34 , pp. 1464-1465
    • Langer, M.1    Pauling, A.2    Rétey, J.3
  • 30
    • 0034160967 scopus 로고    scopus 로고
    • Mechanism and proton activating factors in base-induced β-elimination reactions of N-[2-(4-pyridyl)ethyl]quinuclidinium and N-[2-(2-pyridyl)ethyl]quinuclidinium salts
    • Alunni, S., Conti, A. and Palmizio, ER (2000) Mechanism and proton activating factors in base-induced β-elimination reactions of N-[2-(4-pyridyl)ethyl]quinuclidinium and N-[2-(2-pyridyl)ethyl]quinuclidinium salts. J Chem Soc Perkin Trans, 2, pp. 453-457.
    • (2000) J Chem Soc Perkin Trans , vol.2 , pp. 453-457
    • Alunni, S.1    Conti, A.2    Palmizio, E.R.3
  • 31
    • 0034761096 scopus 로고    scopus 로고
    • Use of solvent isotope effect to identify an intermediate carbanion in the β-elimination reactions from N-[2-(4-pyridyl)ethyl]quinuclidinium and N-[2-(2-pyridyl)ethyl]quinuclidinium induced by acetohydroxamate/ acetohydroxamic acid buffers
    • Alunni, S., Conti, A. and Palmizio, ER (2001) Use of solvent isotope effect to identify an intermediate carbanion in the β-elimination reactions from N-[2-(4-pyridyl)ethyl]quinuclidinium and N-[2-(2-pyridyl)ethyl]quinuclidinium induced by acetohydroxamate/ acetohydroxamic acid buffers. Res Chem Intermed, 27, pp. 635-641.
    • (2001) Res Chem Intermed , vol.27 , pp. 635-641
    • Alunni, S.1    Conti, A.2    Palmizio, E.R.3
  • 32
    • 0035528874 scopus 로고    scopus 로고
    • Mechanism and proton activating factors in base-induced β-elimination reactions of 2-(2-chloroethyl)pyridine
    • Alunni, S. and Busti, A. (2001) Mechanism and proton activating factors in base-induced β-elimination reactions of 2-(2-chloroethyl)pyridine. J Chem Soc Perkin Trans, 2, pp. 778-781.
    • (2001) J Chem Soc Perkin Trans , vol.2 , pp. 778-781
    • Alunni, S.1    Busti, A.2
  • 33
    • 0037423159 scopus 로고    scopus 로고
    • Catalysis of the β-elimination of HF from isomeric 2-fluoroethylpyridines and 1-methyl-2- fluoroethylpyridinium salts
    • Alunni, S., Laureti, V., Ottavi, L. and Ruzziconi, R. (2003) Catalysis of the β-elimination of HF from isomeric 2-fluoroethylpyridines and 1-methyl-2- fluoroethylpyridinium salts. Proton-activating factors and methyl-activating factors as a mechanism test to distinguish between concerted E2 and E1cb irreversible mechanisms. J Org Chem, 68, pp. 718-725.
    • (2003) J Org Chem , vol.68 , pp. 718-725
    • Alunni, S.1    Laureti, V.2    Ottavi, L.3    Ruzziconi, R.4
  • 34
    • 1842452689 scopus 로고    scopus 로고
    • Mechanism of acid-base catalysis of β-elimination reactions in systems activated by a pyridine ring
    • Alunni, S. and Ottavi, L. (2004) Mechanism of acid-base catalysis of β-elimination reactions in systems activated by a pyridine ring. AJ Org Chem, 69, pp. 2272-2283.
    • (2004) AJ Org Chem , vol.69 , pp. 2272-2283
    • Alunni, S.1    Ottavi, L.2
  • 35
    • 27544468690 scopus 로고    scopus 로고
    • Evidence of a borderline region between E1cb and E2 elimination reaction mechanisms: A combined experimental and theorical study of systems activated by the pyridine ring
    • Alunni, S., De Angelis, F., Ottavi, L., Papavasileiou, M. and Tarantelli, F. (2005) Evidence of a borderline region between E1cb and E2 elimination reaction mechanisms: A combined experimental and theorical study of systems activated by the pyridine ring. J Am Chem, 127, pp. 15151-15160.
    • (2005) J Am Chem , vol.127 , pp. 15151-15160
    • Alunni, S.1    De Angelis, F.2    Ottavi, L.3    Papavasileiou, M.4    Tarantelli, F.5
  • 36
    • 0019322677 scopus 로고
    • Adenosine deaminase and adenylate deaminase: Comparative kinect studies with transition state and ground state analog inhibitors
    • Frieden, C., Kurz, LC and Gilbert, HR (1980) Adenosine deaminase and adenylate deaminase: Comparative kinect studies with transition state and ground state analog inhibitors. Biochemistry, 19, pp. 5303-5309.
    • (1980) Biochemistry , vol.19 , pp. 5303-5309
    • Frieden, C.1    Kurz, L.C.2    Gilbert, H.R.3
  • 37
    • 0015514877 scopus 로고
    • Inhibition of adenosine deaminase by alcohols derived from adenine nucleosides
    • Lerner, LM and Rossi, RR (1972) Inhibition of adenosine deaminase by alcohols derived from adenine nucleosides. Biochemistry, 11, pp. 2772-2777.
    • (1972) Biochemistry , vol.11 , pp. 2772-2777
    • Lerner, L.M.1    Rossi, R.R.2
  • 38
    • 0014783142 scopus 로고
    • Structure-activity relationships in adenosine deaminase inhibitors
    • Schaeffer, HJ, Johnson, RN, Odin, E. and Hansch, C. (1970) Structure-activity relationships in adenosine deaminase inhibitors. J Med Chem, 13, pp. 452-455.
    • (1970) J Med Chem , vol.13 , pp. 452-455
    • Schaeffer, H.J.1    Johnson, R.N.2    Odin, E.3    Hansch, C.4
  • 40
    • 0023505886 scopus 로고
    • Kinetic characteristics and binding process of substrate analogs to the adenosine deaminase in the marine mussel, mytilus edulis
    • Ogawa, T., Aikawa, Y. and Aikawa, T. (1987) Kinetic characteristics and binding process of substrate analogs to the adenosine deaminase in the marine mussel, mytilus edulis. Comp Biochem Physiol, 88:1, pp. 91-100.
    • (1987) Comp Biochem Physiol , vol.88 , Issue.1 , pp. 91-100
    • Ogawa, T.1    Aikawa, Y.2    Aikawa, T.3
  • 41
    • 0014525305 scopus 로고
    • On the rate-determining step in the action of adenosine deaminase
    • Wolfenden, R. (1969) On the rate-determining step in the action of adenosine deaminase. Biochemistry, 8:6, pp. 2409-2412.
    • (1969) Biochemistry , vol.8 , Issue.6 , pp. 2409-2412
    • Wolfenden, R.1
  • 42
    • 2442577244 scopus 로고    scopus 로고
    • Inhibition study of adenosine deaminase by caffeine using spectroscopy and isothermal titration calorimetry
    • Saboury, AA, Divsalar, A., Ataie, G., Amanlou, M., Moosavi-Movahedi, AA and Hakimelahi, GH (2003) Inhibition study of adenosine deaminase by caffeine using spectroscopy and isothermal titration calorimetry. Acta Biochem Pol, 50, pp. 849-855.
    • (2003) Acta Biochem Pol , vol.50 , pp. 849-855
    • Saboury, A.A.1    Divsalar, A.2    Ataie, G.3    Amanlou, M.4    Moosavi-Movahedi, A.A.5    Hakimelahi, G.H.6
  • 43
    • 0018846857 scopus 로고
    • The pH-dependence of the inhibitory effects of several divalent cations on the bovine intestine adenosine deaminase activity
    • Aikawa, T., Aikawa, Y. and Brady, TG (1980) The pH-dependence of the inhibitory effects of several divalent cations on the bovine intestine adenosine deaminase activity. Int J Biochem, 12, pp. 493-495.
    • (1980) Int J Biochem , vol.12 , pp. 493-495
    • Aikawa, T.1    Aikawa, Y.2    Brady, T.G.3
  • 44
    • 0004242371 scopus 로고    scopus 로고
    • VCH Publisher, Inc
    • Copeland, A. (1996) Enzymes, VCH Publisher, Inc.
    • (1996) Enzymes
    • Copeland, A.1
  • 45
    • 84960989916 scopus 로고
    • The effect of pH on the affinities of enzymes for substrates and inhibitors
    • Dixon, M. (1953) The effect of pH on the affinities of enzymes for substrates and inhibitors. Biochem J, 55, pp. 161-170.
    • (1953) Biochem J , vol.55 , pp. 161-170
    • Dixon, M.1
  • 46
    • 0004105856 scopus 로고
    • Langman Scientific and Technical, Harlow, Essex, England
    • Isaac, NS (1987) Physical organic chemistry, Langman Scientific and Technical, Harlow, Essex, England
    • (1987) Physical Organic Chemistry
    • Isaac, N.S.1
  • 47
    • 0000372840 scopus 로고
    • α-effects IV. Additional observation on the α;-effect employing malachite green as substrate
    • Bruice, TC and Dixon, JE (1971) α-effects IV. Additional observation on the α;-effect employing malachite green as substrate. J Am Chem Soc, 93, pp. 6592-6597.
    • (1971) J Am Chem Soc , vol.93 , pp. 6592-6597
    • Bruice, T.C.1    Dixon, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.