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Volumn 73, Issue 7, 2007, Pages 981-989

Structure and function of eritadenine and its 3-deaza analogues: Potent inhibitors of S-adenosylhomocysteine hydrolase and hypocholesterolemic agents

Author keywords

3 Deaza analogue; Chemical synthesis; Cholesterol reduction; Enzyme inhibition; Eritadenine; S Adenosylhomocysteine hydrolase

Indexed keywords

4 (3 DEAZAADENIN 9 YL) 2,3 DIHYDROXYBUTANOIC ACID; ADENOSINE DEAMINASE; ADENOSYLHOMOCYSTEINASE; ADENOSYLHOMOCYSTEINASE INHIBITOR; CHOLESTEROL; ERITADENINE; GLYCOSIDE; HYPOCHOLESTEROLEMIC AGENT; METHYL 4 (3 DEAZAADENIN 9 YL) 2,3 DIHYDROXYBUTANOATE; N METHYL 4 (3 DEAZAADENIN 9 YL) 2,3 DIHYDROXYBUTANAMIDE; PHOSPHOLIPID; TRIACYLGLYCEROL; UNCLASSIFIED DRUG;

EID: 33847127806     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2006.12.014     Document Type: Article
Times cited : (27)

References (39)
  • 1
    • 0028096810 scopus 로고
    • A review of clinical trials comparing HMG-CoA reductase inhibitors
    • Illingworth D.R., and Tobert J.A. A review of clinical trials comparing HMG-CoA reductase inhibitors. Clin Ther 16 (1994) 366-385
    • (1994) Clin Ther , vol.16 , pp. 366-385
    • Illingworth, D.R.1    Tobert, J.A.2
  • 2
    • 0023879854 scopus 로고
    • Effects of fibrates on serum lipids and atherosclerosis
    • Sirtori C.R., and Franceschini G. Effects of fibrates on serum lipids and atherosclerosis. Pharmacol Ther 37 (1988) 167-191
    • (1988) Pharmacol Ther , vol.37 , pp. 167-191
    • Sirtori, C.R.1    Franceschini, G.2
  • 4
    • 33747722742 scopus 로고    scopus 로고
    • Raloxifene increases proliferation and upregulates telomerase activity in human umbilical vein endothelial cells
    • Doshida M., Ohmichi M., Tsutsumi S., Kawagoe J., Takahashi T., Du B., et al. Raloxifene increases proliferation and upregulates telomerase activity in human umbilical vein endothelial cells. J Biol Chem 281 (2006) 24270-24278
    • (2006) J Biol Chem , vol.281 , pp. 24270-24278
    • Doshida, M.1    Ohmichi, M.2    Tsutsumi, S.3    Kawagoe, J.4    Takahashi, T.5    Du, B.6
  • 5
    • 2642712522 scopus 로고    scopus 로고
    • Effects of raloxifene on serum lipids and coagulation factors in healthy postmenopausal women
    • Walsh B.W., Kuller L.H., Wild R.A., Paul S., Farmer M., Lawrence J.B., et al. Effects of raloxifene on serum lipids and coagulation factors in healthy postmenopausal women. JAMA 279 (1998) 1445-1451
    • (1998) JAMA , vol.279 , pp. 1445-1451
    • Walsh, B.W.1    Kuller, L.H.2    Wild, R.A.3    Paul, S.4    Farmer, M.5    Lawrence, J.B.6
  • 6
    • 0028326125 scopus 로고
    • ACAT inhibitors as antiatherosclerotic agents: compounds and mechanisms
    • Matsuda K. ACAT inhibitors as antiatherosclerotic agents: compounds and mechanisms. Med Res Rev 14 (1994) 271-305
    • (1994) Med Res Rev , vol.14 , pp. 271-305
    • Matsuda, K.1
  • 7
  • 8
    • 0022256566 scopus 로고
    • Role of acyl-CoA: cholesterol acyltransferase in cellular cholesterol metabolism
    • Suckling K.E., and Stange E.F. Role of acyl-CoA: cholesterol acyltransferase in cellular cholesterol metabolism. J Lipid Res 26 (1985) 647-671
    • (1985) J Lipid Res , vol.26 , pp. 647-671
    • Suckling, K.E.1    Stange, E.F.2
  • 9
    • 0001324937 scopus 로고
    • Arterial cholesterol esterification by acyl CoAcholesterol acyltransferase: its possible significance in atherogenesis and its inhibition by drugs
    • Fears R., Levy R.I., Shepard J., Packard C.J., and Miller N.E. (Eds), J.R. Prous Science Publishers, Spain
    • Bell F.P. Arterial cholesterol esterification by acyl CoAcholesterol acyltransferase: its possible significance in atherogenesis and its inhibition by drugs. In: Fears R., Levy R.I., Shepard J., Packard C.J., and Miller N.E. (Eds). Pharmacological control of hyperlipidaemia (1986), J.R. Prous Science Publishers, Spain 409-422
    • (1986) Pharmacological control of hyperlipidaemia , pp. 409-422
    • Bell, F.P.1
  • 10
    • 0025756150 scopus 로고
    • Therapeutic potential of ACAT inhibitors as lipid lowering and anti-atherosclerotic agents
    • Sliskovic D.R., and White A.D. Therapeutic potential of ACAT inhibitors as lipid lowering and anti-atherosclerotic agents. Trends Pharmacol Sci 12 (1991) 194-199
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 194-199
    • Sliskovic, D.R.1    White, A.D.2
  • 11
    • 0014680224 scopus 로고
    • Lentinacin: a new hypocholesterolemic substance in Lentinus edodes
    • Chibata I., Okumura K., Takeyama S., and Kotera K. Lentinacin: a new hypocholesterolemic substance in Lentinus edodes. Experientia 25 (1969) 1237-1238
    • (1969) Experientia , vol.25 , pp. 1237-1238
    • Chibata, I.1    Okumura, K.2    Takeyama, S.3    Kotera, K.4
  • 14
    • 0021688433 scopus 로고
    • The effect of aliphatic adenine analogues on S-adenosylhomocysteine and S-adenosylhomocysteine hydrolase in intact rat hepatocytes
    • Schanche J.S., Schanche T., Ueland P.M., Holy A., and Votruba I. The effect of aliphatic adenine analogues on S-adenosylhomocysteine and S-adenosylhomocysteine hydrolase in intact rat hepatocytes. Mol Pharmacol 26 (1984) 553-558
    • (1984) Mol Pharmacol , vol.26 , pp. 553-558
    • Schanche, J.S.1    Schanche, T.2    Ueland, P.M.3    Holy, A.4    Votruba, I.5
  • 15
    • 0027988220 scopus 로고
    • High recombinagenic activities of three antiviral agents, adenine derivatives, in the Drosophila wing spot test
    • Marec F., and Gelbic I. High recombinagenic activities of three antiviral agents, adenine derivatives, in the Drosophila wing spot test. Mutat Res 311 (1994) 305-317
    • (1994) Mutat Res , vol.311 , pp. 305-317
    • Marec, F.1    Gelbic, I.2
  • 16
    • 0024969637 scopus 로고
    • Inhibition of phosphatase by open-chain nucleoside analogues in insects
    • Nemec V., and Slama K. Inhibition of phosphatase by open-chain nucleoside analogues in insects. Experientia 45 (1989) 148-150
    • (1989) Experientia , vol.45 , pp. 148-150
    • Nemec, V.1    Slama, K.2
  • 17
    • 0036510742 scopus 로고    scopus 로고
    • Inhibition of S-adenosylhomocysteine hydrolase by "acyclic sugar" adenosine analogue d-eritadenine: crystal structure of S-adenosylhomocysteine hydrolase complexed with d-eritadenine
    • Huang Y., Komoto J., Takata Y., Powell D.R., Gomi T., Ogawa H., et al. Inhibition of S-adenosylhomocysteine hydrolase by "acyclic sugar" adenosine analogue d-eritadenine: crystal structure of S-adenosylhomocysteine hydrolase complexed with d-eritadenine. J Biol Chem 277 (2002) 7477-7482
    • (2002) J Biol Chem , vol.277 , pp. 7477-7482
    • Huang, Y.1    Komoto, J.2    Takata, Y.3    Powell, D.R.4    Gomi, T.5    Ogawa, H.6
  • 18
    • 0034741683 scopus 로고    scopus 로고
    • 3′-Deoxyribofuranose derivatives of 1-deaza and 3-deaza-adenosine and their activity as adenosine deaminase inhibitors
    • Costanzi S., Lambertucci C., Volpini R., Vittori S., Lupidi G., and Cristalli G. 3′-Deoxyribofuranose derivatives of 1-deaza and 3-deaza-adenosine and their activity as adenosine deaminase inhibitors. Nucleos Nucleot Nucl Acids 20 (2001) 1037-1041
    • (2001) Nucleos Nucleot Nucl Acids , vol.20 , pp. 1037-1041
    • Costanzi, S.1    Lambertucci, C.2    Volpini, R.3    Vittori, S.4    Lupidi, G.5    Cristalli, G.6
  • 19
    • 0035853293 scopus 로고    scopus 로고
    • Structure and function of a novel purine specific nucleoside hydrolase from Trypanosoma vivax
    • Verseés W., Decanniere K., Pelleé R., Depoorter J., Brosens E., Parkin D.W., et al. Structure and function of a novel purine specific nucleoside hydrolase from Trypanosoma vivax. J Mol Biol 307 (2001) 1363-1379
    • (2001) J Mol Biol , vol.307 , pp. 1363-1379
    • Verseés, W.1    Decanniere, K.2    Pelleé, R.3    Depoorter, J.4    Brosens, E.5    Parkin, D.W.6
  • 20
    • 0001453542 scopus 로고
    • Synthesis of various chloroimidazo[4,5-c] pyridines and related derivatives (1)
    • Rousseau R.J., and Robins R.K. Synthesis of various chloroimidazo[4,5-c] pyridines and related derivatives (1). J Heterocycl Chem 2 (1965) 196-201
    • (1965) J Heterocycl Chem , vol.2 , pp. 196-201
    • Rousseau, R.J.1    Robins, R.K.2
  • 21
    • 84944171619 scopus 로고
    • Deazapurine derivatives. V. New synthesis of 1- and 3-deaza-adenine and related compounds
    • De Roos K.B., and Salemink C.A. Deazapurine derivatives. V. New synthesis of 1- and 3-deaza-adenine and related compounds. Rec Trav Chim Pays-Bas 88 (1969) 1263-1274
    • (1969) Rec Trav Chim Pays-Bas , vol.88 , pp. 1263-1274
    • De Roos, K.B.1    Salemink, C.A.2
  • 22
    • 0015231049 scopus 로고
    • Synthetic studies on eritadenine. I. Reactions of some purines with the 2,3-O-protected dihydroxybutyrolactone
    • Okumura K., Oine T., Yamada Y., Tomie M., Adachi T., Nagura T., et al. Synthetic studies on eritadenine. I. Reactions of some purines with the 2,3-O-protected dihydroxybutyrolactone. J Org Chem 36 (1971) 1573-1579
    • (1971) J Org Chem , vol.36 , pp. 1573-1579
    • Okumura, K.1    Oine, T.2    Yamada, Y.3    Tomie, M.4    Adachi, T.5    Nagura, T.6
  • 23
    • 21144460188 scopus 로고
    • Synthesis and biological effects of acyclic analogs of deazapurine nucleosides
    • Dvorakova H., Holy A., Votruba I., and Masojidkova M. Synthesis and biological effects of acyclic analogs of deazapurine nucleosides. Collect Czech Chem Commun 58 (1993) 629-648
    • (1993) Collect Czech Chem Commun , vol.58 , pp. 629-648
    • Dvorakova, H.1    Holy, A.2    Votruba, I.3    Masojidkova, M.4
  • 24
    • 0024418257 scopus 로고
    • Expression of rat liver S-adenosylhomocysteinase cDNA in Escherichia coli and mutagenesis at the putative NAD binding site
    • Gomi T., Date T., Ogawa H., Fujioka M., Aksamit R.R., Backlund P.S., et al. Expression of rat liver S-adenosylhomocysteinase cDNA in Escherichia coli and mutagenesis at the putative NAD binding site. J Biol Chem 264 (1989) 16138-16142
    • (1989) J Biol Chem , vol.264 , pp. 16138-16142
    • Gomi, T.1    Date, T.2    Ogawa, H.3    Fujioka, M.4    Aksamit, R.R.5    Backlund, P.S.6
  • 25
    • 0019887737 scopus 로고
    • S-Adenosylhomocysteine hydrolase from rat liver. Purification and some properties
    • Fujioka M., and Takata Y. S-Adenosylhomocysteine hydrolase from rat liver. Purification and some properties. J Biol Chem 256 (1981) 1631-1635
    • (1981) J Biol Chem , vol.256 , pp. 1631-1635
    • Fujioka, M.1    Takata, Y.2
  • 26
    • 0017375321 scopus 로고    scopus 로고
    • American Institute of Nutrition. Report of the American Institute of Nutrition ad hoc committee on standards for nutritional studies. J Nutr 1977;107:1340-48.
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276 (1997) 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 0000243829 scopus 로고
    • ROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. ROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26 (1993) 283-291
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 30
    • 0033614793 scopus 로고    scopus 로고
    • Crystal structure of S-adenosylhomocysteine hydrolase from rat liver
    • Hu Y., Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., et al. Crystal structure of S-adenosylhomocysteine hydrolase from rat liver. Biochemistry 38 (1999) 8323-8333
    • (1999) Biochemistry , vol.38 , pp. 8323-8333
    • Hu, Y.1    Komoto, J.2    Huang, Y.3    Gomi, T.4    Ogawa, H.5    Takata, Y.6
  • 31
    • 0034644738 scopus 로고    scopus 로고
    • Effects of site-directed mutagenesis on the structure of S-adenosylhomocysteine hydrolase: crystal structure of D244E Mutant enzyme
    • Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M., et al. Effects of site-directed mutagenesis on the structure of S-adenosylhomocysteine hydrolase: crystal structure of D244E Mutant enzyme. J Biol Chem 275 (2000) 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
  • 32
    • 23944456820 scopus 로고    scopus 로고
    • Catalytic mechanism of S-adenosylhomocysteine hydrolase: roles of His 54, Asp130, Glu155, Lys185, and Asp189
    • Yamada T., Takata Y., Komoto J., Gomi T., Ogawa H., Fujioka M., et al. Catalytic mechanism of S-adenosylhomocysteine hydrolase: roles of His 54, Asp130, Glu155, Lys185, and Asp189. Int J Biochem Cell Biol 37 (2005) 2417-2435
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 2417-2435
    • Yamada, T.1    Takata, Y.2    Komoto, J.3    Gomi, T.4    Ogawa, H.5    Fujioka, M.6
  • 33
    • 0038016563 scopus 로고    scopus 로고
    • Synthesis and biological activity of novel S-adenosyl-l-homocysteine hydrolase inhibitors
    • Steereand J.A., and Honek J.F. Synthesis and biological activity of novel S-adenosyl-l-homocysteine hydrolase inhibitors. Bioorg Med Chem 11 (2003) 3229-3236
    • (2003) Bioorg Med Chem , vol.11 , pp. 3229-3236
    • Steereand, J.A.1    Honek, J.F.2
  • 34
    • 0025123336 scopus 로고
    • Site-directed mutagenesis of rat liver S-adenosylhomocysteinase. Effect of conversion of aspartic acid 244 to glutamic acid on coenzyme binding
    • Gomi T., Takata Y., Date T., Fujioka M., Aksamit R.R., Backlund Jr. P.S., et al. Site-directed mutagenesis of rat liver S-adenosylhomocysteinase. Effect of conversion of aspartic acid 244 to glutamic acid on coenzyme binding. J. Biol Chem 265 (1990) 16102-16107
    • (1990) J. Biol Chem , vol.265 , pp. 16102-16107
    • Gomi, T.1    Takata, Y.2    Date, T.3    Fujioka, M.4    Aksamit, R.R.5    Backlund Jr., P.S.6
  • 35
    • 0027398949 scopus 로고
    • A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water
    • Wilson D.K., and Quiocho F.A. A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water. Biochemistry 32 (1993) 1689-1694
    • (1993) Biochemistry , vol.32 , pp. 1689-1694
    • Wilson, D.K.1    Quiocho, F.A.2
  • 36
    • 0041322993 scopus 로고    scopus 로고
    • Anti-HIV-1 activity of 3-deaza-adenosine analogs inhibition of S-adenosylhomocysteine hydrolase and nucleotide congeners
    • Gordon R.K., Ginalsk K., Rudnicki W.R., Rychlewski L., Pankaskie M.C., Bujnicki J.M., et al. Anti-HIV-1 activity of 3-deaza-adenosine analogs inhibition of S-adenosylhomocysteine hydrolase and nucleotide congeners. Eur J Biochem 270 (2003) 3507-3517
    • (2003) Eur J Biochem , vol.270 , pp. 3507-3517
    • Gordon, R.K.1    Ginalsk, K.2    Rudnicki, W.R.3    Rychlewski, L.4    Pankaskie, M.C.5    Bujnicki, J.M.6
  • 37
    • 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., et al. Catalytic strategy of S-adenosyl-l-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions. Biochemistry 42 (2003) 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
  • 38
    • 1542440250 scopus 로고    scopus 로고
    • Eritadenine-induced alterations of plasma lipoprotein lipid concentrations and phosphatidylcholine molecular species profile in rats fed cholesterol-free and cholesterol-enriched diets
    • Shimada Y., Morita X., and Sugiyama K. Eritadenine-induced alterations of plasma lipoprotein lipid concentrations and phosphatidylcholine molecular species profile in rats fed cholesterol-free and cholesterol-enriched diets. Biosci Biotechnol Biochem 67 (2003) 996-1006
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 996-1006
    • Shimada, Y.1    Morita, X.2    Sugiyama, K.3
  • 39
    • 0001196262 scopus 로고
    • Multiple range tests for correlated and heteroscedastic means
    • Duncan D.B. Multiple range tests for correlated and heteroscedastic means. Biometrics 13 (1957) 164-176
    • (1957) Biometrics , vol.13 , pp. 164-176
    • Duncan, D.B.1


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