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Volumn 66, Issue 11, 2003, Pages 2117-2123

Adenosine binding sites at S-adenosylhomocysteine hydrolase are controlled by the NAD+/NADH ratio of the enzyme

Author keywords

Adenosine binding sites; Apo enzyme; Azido adenosine; NAD+ NADH ratio; Photolabeled peptides; S Adenosylhomocysteine hydrolase

Indexed keywords

ADENOSINE; ADENOSYLHOMOCYSTEINASE; ALANINE; ASPARAGINE; ENZYME; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PEPTIDE; PEPTIDE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; THREONINE; TYROSINE DERIVATIVE; VALINE;

EID: 0242492176     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(03)00581-1     Document Type: Article
Times cited : (17)

References (33)
  • 1
    • 0002616156 scopus 로고
    • The role of S-adenosylhomocysteine and S-adenosylhomocysteine hydrolase in the control of biological methylation
    • Cavallini D, Gaull GE, Zappia V., editors. New York and London: Plenum Press
    • Cantoni GL, Chiang PK. The role of S-adenosylhomocysteine and S-adenosylhomocysteine hydrolase in the control of biological methylation. In: Cavallini D, Gaull GE, Zappia V., editors. Natural sulfur compounds: novel biochemical and structural aspects. New York and London: Plenum Press; 1980. p. 67-80.
    • (1980) Natural sulfur compounds: novel biochemical and structural aspects , pp. 67-80
    • Cantoni, G.L.1    Chiang, P.K.2
  • 2
    • 0021212302 scopus 로고
    • Inhibition of protein carboxyl methylation by S-adenosyl-L-homocysteine in intact erythrocytes. Physiological consequences
    • Barber J.R., Clarke S. Inhibition of protein carboxyl methylation by S-adenosyl-L-homocysteine in intact erythrocytes. Physiological consequences. J. Biol. Chem. 259:1984;7115-7122.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7115-7122
    • Barber, J.R.1    Clarke, S.2
  • 3
    • 0019417904 scopus 로고
    • Decreased transmethylation of biogenic amines after in vivo elevation of brain S-adenosyl-L-homocysteine
    • Schatz R.A., Wilens T.E., Sellinger O.Z. Decreased transmethylation of biogenic amines after in vivo elevation of brain S-adenosyl-L-homocysteine. J. Neurochem. 36:1981;1739-1748.
    • (1981) J. Neurochem. , vol.36 , pp. 1739-1748
    • Schatz, R.A.1    Wilens, T.E.2    Sellinger, O.Z.3
  • 4
    • 0000085851 scopus 로고
    • The role of adenosine in the regulation of glomerular filtration rate and renin secretion
    • Osswald H. The role of adenosine in the regulation of glomerular filtration rate and renin secretion. TIPS. 5:1984;94-97.
    • (1984) TIPS , vol.5 , pp. 94-97
    • Osswald, H.1
  • 5
    • 0025836491 scopus 로고
    • Adenosine mediates tubuloglomerular feedback response: An element of metabolic control of kidney function
    • Osswald H., Mühlbauer B., Schenk F. Adenosine mediates tubuloglomerular feedback response: an element of metabolic control of kidney function. Kidney Int. 39:1991;128-131.
    • (1991) Kidney Int. , vol.39 , pp. 128-131
    • Osswald, H.1    Mühlbauer, B.2    Schenk, F.3
  • 6
    • 0027366776 scopus 로고
    • Rapid turnover of the AMP-adenosine metabolic cycle in the guinea pig heart
    • Kroll K., Decking U.K., Dreikorn K., Schrader J. Rapid turnover of the AMP-adenosine metabolic cycle in the guinea pig heart. Circ. Res. 73:1993;846-856.
    • (1993) Circ. Res. , vol.73 , pp. 846-856
    • Kroll, K.1    Decking, U.K.2    Dreikorn, K.3    Schrader, J.4
  • 7
    • 0018875426 scopus 로고
    • Modulation of neurotransmission by purine nucleotides and nucleosides
    • Fredholm B.B., Hedqvist P. Modulation of neurotransmission by purine nucleotides and nucleosides. Biochem. Pharmacol. 29:1980;1635-1643.
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 1635-1643
    • Fredholm, B.B.1    Hedqvist, P.2
  • 8
    • 0033620779 scopus 로고    scopus 로고
    • Homocysteine and vascular disease
    • Hankey G.J., Eickelboom J.W. Homocysteine and vascular disease. Lancet. 354:1999;407-413.
    • (1999) Lancet , vol.354 , pp. 407-413
    • Hankey, G.J.1    Eickelboom, J.W.2
  • 9
    • 0017224213 scopus 로고
    • Capping of eukaryotic mRNAs
    • Shatkin A.J. Capping of eukaryotic mRNAs. Cell. 9:1976;645-653.
    • (1976) Cell , vol.9 , pp. 645-653
    • Shatkin, A.J.1
  • 10
    • 0021220516 scopus 로고
    • Methionine metabolism in mammals. Distribution of homocysteine between competing pathways
    • Finkelstein J.D., Martin J.J. Methionine metabolism in mammals. Distribution of homocysteine between competing pathways. J. Biol. Chem. 259:1984;9508-9513.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9508-9513
    • Finkelstein, J.D.1    Martin, J.J.2
  • 12
    • 0018800321 scopus 로고
    • Mechanism of action of S-adenosylhomocysteinase
    • Palmer J.L., Abeles R.H. Mechanism of action of S-adenosylhomocysteinase. J. Biol. Chem. 254:1979;1217-1226.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1217-1226
    • Palmer, J.L.1    Abeles, R.H.2
  • 13
    • 0031947190 scopus 로고    scopus 로고
    • Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength
    • Turner M.A., Yuan C.S., Borchardt R.T., Hershfield M.S., Smith G.D., Howell P.L. Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nature Struc. Biol. 5:1998;369-376.
    • (1998) Nature Struc. Biol. , vol.5 , pp. 369-376
    • Turner, M.A.1    Yuan, C.S.2    Borchardt, R.T.3    Hershfield, M.S.4    Smith, G.D.5    Howell, P.L.6
  • 14
    • 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., Fujioka M., Takusagawa F. 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    Fujioka, M.7    Takusagawa, F.8
  • 15
    • 0026701908 scopus 로고
    • Reduced S-adenosylhomocysteine hydrolase. Kinetics and thermodynamics for binding of 3′-ketoadenosine, adenosine, and adenine
    • Porter D.J.T., Boyd F.L. Reduced S-adenosylhomocysteine hydrolase. Kinetics and thermodynamics for binding of 3′-ketoadenosine, adenosine, and adenine. J. Biol. Chem. 267:1992;3205-3213.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3205-3213
    • Porter, D.J.T.1    Boyd, F.L.2
  • 16
    • 0034033802 scopus 로고    scopus 로고
    • Simple and sensitive binding assay for measurement of adenosine using reduced S-adenosylhomocysteine hydrolase
    • Kloor D., Kozo Y., Delabar U., Osswald H. Simple and sensitive binding assay for measurement of adenosine using reduced S-adenosylhomocysteine hydrolase. Clin. Chem. 46:2000;537-542.
    • (2000) Clin. Chem. , vol.46 , pp. 537-542
    • Kloor, D.1    Kozo, Y.2    Delabar, U.3    Osswald, H.4
  • 17
    • 0029658566 scopus 로고    scopus 로고
    • S-Adenosylhomocysteine hydrolase from bovine kidney: Enzymatic and binding properties
    • Kloor D., Fuchs S., Kurz J., Faust B., Osswald H. S-Adenosylhomocysteine hydrolase from bovine kidney: enzymatic and binding properties. Kidney Blood Press. Res. 19:1996;100-108.
    • (1996) Kidney Blood Press. Res. , vol.19 , pp. 100-108
    • Kloor, D.1    Fuchs, S.2    Kurz, J.3    Faust, B.4    Osswald, H.5
  • 18
    • 0017863232 scopus 로고
    • Ligand binding to the adenosine analogue binding protein in rabbit erythrocyte
    • Olsson R.A. Ligand binding to the adenosine analogue binding protein in rabbit erythrocyte. Biochemistry. 17:1978;367-375.
    • (1978) Biochemistry , vol.17 , pp. 367-375
    • Olsson, R.A.1
  • 19
    • 0018075296 scopus 로고
    • S-Adenosylhomocysteine hydrolase is an adenosine binding protein: A target for adenosine toxicity
    • Hershfield M.S., Kredich N.M. S-Adenosylhomocysteine hydrolase is an adenosine binding protein: a target for adenosine toxicity. Science. 202:1978;757-760.
    • (1978) Science , vol.202 , pp. 757-760
    • Hershfield, M.S.1    Kredich, N.M.2
  • 20
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0020679964 scopus 로고
    • Protein sequence analysis: Automated microsequencing
    • Hunkapiller M.W., Hood L.E. Protein sequence analysis: automated microsequencing. Science. 219:1983;650-659.
    • (1983) Science , vol.219 , pp. 650-659
    • Hunkapiller, M.W.1    Hood, L.E.2
  • 22
    • 0025677738 scopus 로고
    • Mass spectrometry of peptides and proteins by matrix-assisted ultraviolet laser desorption/ionization
    • Hillenkamp F., Karas M. Mass spectrometry of peptides and proteins by matrix-assisted ultraviolet laser desorption/ionization. Methods Enzymol. 193:1990;280-295.
    • (1990) Methods Enzymol. , vol.193 , pp. 280-295
    • Hillenkamp, F.1    Karas, M.2
  • 23
    • 0031283298 scopus 로고    scopus 로고
    • Peptides adsorbed on reverse-phase femtomole sequencing by post-source decay matrix assisted laser desorption ionization-reflectron time of flight mass spectrometry (MALDI-RETOF-MS)
    • Gevaert K., Demol H., Puype M., Broekaert D., De Boek S., Houthaeve T., Vandekerckhove J. Peptides adsorbed on reverse-phase femtomole sequencing by post-source decay matrix assisted laser desorption ionization-reflectron time of flight mass spectrometry (MALDI-RETOF-MS). Electrophoresis. 18:1997;2950-2960.
    • (1997) Electrophoresis , vol.18 , pp. 2950-2960
    • Gevaert, K.1    Demol, H.2    Puype, M.3    Broekaert, D.4    De Boek, S.5    Houthaeve, T.6    Vandekerckhove, J.7
  • 24
    • 0019061918 scopus 로고
    • LIGAND: A versatile computerized approach for the characterization of ligand binding systems
    • Munson P.J., Rodbard D. LIGAND: a versatile computerized approach for the characterization of ligand binding systems. Anal. Biochem. 107:1980;220-239.
    • (1980) Anal. Biochem. , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 26
    • 0034644738 scopus 로고    scopus 로고
    • Effects of site-directed mutagenesis on structure and function of recombinant rat liver S-adenosylhomocysteine hydrolase
    • Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M., Takusagawa F. Effects of site-directed mutagenesis on structure and function of recombinant rat liver S-adenosylhomocysteine hydrolase. 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    Takusagawa, F.7
  • 28
    • 0037085042 scopus 로고    scopus 로고
    • Tissue levels of S-adenosylhomocysteine in the rat kidney: Effects of ischemia and homocysteine
    • Kloor D., Delabar U., Mühlbauer B., Luippold G., Osswald H. Tissue levels of S-adenosylhomocysteine in the rat kidney: effects of ischemia and homocysteine. Biochem. Pharmacol. 63:2002;809-815.
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 809-815
    • Kloor, D.1    Delabar, U.2    Mühlbauer, B.3    Luippold, G.4    Osswald, H.5
  • 29
    • 0037107611 scopus 로고    scopus 로고
    • Characterization of the cAMP binding site of purified S-adenosylhomocysteine hydrolase from bovine kidney
    • Kloor D., Danielyan L., Osswald H. Characterization of the cAMP binding site of purified S-adenosylhomocysteine hydrolase from bovine kidney. Biochem. Pharmacol. 64:2002;1201-1206.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1201-1206
    • Kloor, D.1    Danielyan, L.2    Osswald, H.3
  • 31
    • 0031738238 scopus 로고    scopus 로고
    • Effects of ions on adenosine binding and enzyme activity of purified S-adenosylhomocysteine hydrolase from bovine kidney
    • Kloor D., Fuchs S., Petroktistis F., Delabar U., Mühlbauer B., Quast U., Osswald H. Effects of ions on adenosine binding and enzyme activity of purified S-adenosylhomocysteine hydrolase from bovine kidney. Biochem. Pharmacol. 56:1998;1493-1496.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 1493-1496
    • Kloor, D.1    Fuchs, S.2    Petroktistis, F.3    Delabar, U.4    Mühlbauer, B.5    Quast, U.6    Osswald, H.7
  • 32
    • 0031871194 scopus 로고    scopus 로고
    • Mechanism of extracellular ATP- and adenosine-induced apoptosis of cultured pulmonary artery endothelial cells
    • Rounds S., Yee L.W., Dawicki D.D., Harrington E., Parks N., Cutaia M.V. Mechanism of extracellular ATP- and adenosine-induced apoptosis of cultured pulmonary artery endothelial cells. Am. J. Physiol. 275:1998;L378-L388.
    • (1998) Am. J. Physiol. , vol.275
    • Rounds, S.1    Yee, L.W.2    Dawicki, D.D.3    Harrington, E.4    Parks, N.5    Cutaia, M.V.6


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