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Volumn 348, Issue 3, 2000, Pages 579-583

Contrasting effects of N5-substituted tetrahydrobiopterin derivatives on phenylalanine hydroxylase, dihydropteridine reductase and nitric oxide synthase

Author keywords

Biopterin; Inhibition; Reaction mechanism; Redox cycling; Stimulation

Indexed keywords

2,6 DICHLOROPHENOLINDOPHENOL; ACETIC ACID; DIHYDROPTERIDINE REDUCTASE; FORMIC ACID; METHYL GROUP; NITRIC OXIDE SYNTHASE; PHENYLALANINE 4 MONOOXYGENASE; RECOMBINANT ENZYME; TETRAHYDROBIOPTERIN; 5,6,7,8-TETRAHYDROBIOPTERIN; BIOPTERIN; DRUG DERIVATIVE; NEURONAL NITRIC OXIDE SYNTHASE; NOS1 PROTEIN, RAT; RECOMBINANT PROTEIN;

EID: 0034659806     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3480579     Document Type: Article
Times cited : (14)

References (33)
  • 1
    • 0027267693 scopus 로고
    • New tetrahydrobiopterin-dependent systems
    • 1 Kaufman, S. (1993) New tetrahydrobiopterin-dependent systems. Annu. Rev. Nutr. 13, 261-286
    • (1993) Annu. Rev. Nutr. , vol.13 , pp. 261-286
    • Kaufman, S.1
  • 2
    • 0024351625 scopus 로고
    • Reduced biopterin as a cofactor in the generation of nitrogen oxides by murine macrophages
    • 2 Kwon, N. S., Nathan, C. F. and Stuehr, D. J. (1989) Reduced biopterin as a cofactor in the generation of nitrogen oxides by murine macrophages. J. Biol. Chem. 264, 20496-20501
    • (1989) J. Biol. Chem. , vol.264 , pp. 20496-20501
    • Kwon, N.S.1    Nathan, C.F.2    Stuehr, D.J.3
  • 3
    • 0029827739 scopus 로고    scopus 로고
    • Identification of the 4-amino analogue of tetrahydrobiopterin as a dihydropteridine reductase inhibitor and a potent pteridine antagonist of rat neuronal nitric oxide synthase
    • 3 Werner, E. R., Pitters, E., Schmidt, K., Wachter, H., Werner-Felmayer, G. and Mayer, B. (1996) Identification of the 4-amino analogue of tetrahydrobiopterin as a dihydropteridine reductase inhibitor and a potent pteridine antagonist of rat neuronal nitric oxide synthase. Biochem. J. 320, 193-196
    • (1996) Biochem. J. , vol.320 , pp. 193-196
    • Werner, E.R.1    Pitters, E.2    Schmidt, K.3    Wachter, H.4    Werner-Felmayer, G.5    Mayer, B.6
  • 4
    • 0028302095 scopus 로고
    • The pteridine binding site of brain nitric oxide synthase - Tetrahydrobiopterin binding kinetics, specificity, and allosteric interaction with the substrate domain
    • 4 Klatt, P., Schmid, M., Leopold, E., Schmidt, K., Werner, E. R. and Mayer, B. (1994) The pteridine binding site of brain nitric oxide synthase - tetrahydrobiopterin binding kinetics, specificity, and allosteric interaction with the substrate domain. J. Biol. Chem. 269, 13861-13866
    • (1994) J. Biol. Chem. , vol.269 , pp. 13861-13866
    • Klatt, P.1    Schmid, M.2    Leopold, E.3    Schmidt, K.4    Werner, E.R.5    Mayer, B.6
  • 5
    • 0032488596 scopus 로고    scopus 로고
    • Comparative functioning of dihydro- and tetrahydropterins in supporting electron transfer, catalysis, and subunit dimerization in inducible nitric oxide synthase
    • 5 Presta, A., Siddhanta, U., Wu, C. Q., Sennequier, N., Huang, L. X., Abusoud, H. M., Erzurum, S. and Stuehr, D. J. (1998) Comparative functioning of dihydro-and tetrahydropterins in supporting electron transfer, catalysis, and subunit dimerization in inducible nitric oxide synthase. Biochemistry 37, 298-310
    • (1998) Biochemistry , vol.37 , pp. 298-310
    • Presta, A.1    Siddhanta, U.2    Wu, C.Q.3    Sennequier, N.4    Huang, L.X.5    Abusoud, H.M.6    Erzurum, S.7    Stuehr, D.J.8
  • 6
    • 0027441142 scopus 로고
    • Macrophage nitric oxide synthase subunits - Purification, characterization, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme
    • 6 Baek, K. J., Thiel, B. A., Lucas, S. and Stuehr, D. J. (1993) Macrophage nitric oxide synthase subunits - purification, characterization, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme. J. Biol. Chem. 268, 21120-21129
    • (1993) J. Biol. Chem. , vol.268 , pp. 21120-21129
    • Baek, K.J.1    Thiel, B.A.2    Lucas, S.3    Stuehr, D.J.4
  • 7
    • 0029125762 scopus 로고
    • Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer
    • 7 Klatt, P., Schmidt, K., Lehner, D., Glatter, O., Bachinger, H. P. and Mayer, B. (1995) Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer. EMBO J. 14, 3687-3695
    • (1995) EMBO J. , vol.14 , pp. 3687-3695
    • Klatt, P.1    Schmidt, K.2    Lehner, D.3    Glatter, O.4    Bachinger, H.P.5    Mayer, B.6
  • 8
    • 0030948345 scopus 로고    scopus 로고
    • Characterization of bovine endothelial nitric oxide synthase as a homodimer with down-regulated uncoupled NADPH oxidase activity: Tetrahydrobiopterin binding kinetics and role of haem in dimerization
    • 8 List, B. M., Klosch, B., Volker, C., Gorren, A. C., Sessa, W. C., Werner, E. R., Kukovelz, W. R., Schmidt, K. and Mayer, B. (1997) Characterization of bovine endothelial nitric oxide synthase as a homodimer with down-regulated uncoupled NADPH oxidase activity: tetrahydrobiopterin binding kinetics and role of haem in dimerization. Biochem. J. 323, 159-165
    • (1997) Biochem. J. , vol.323 , pp. 159-165
    • List, B.M.1    Klosch, B.2    Volker, C.3    Gorren, A.C.4    Sessa, W.C.5    Werner, E.R.6    Kukovelz, W.R.7    Schmidt, K.8    Mayer, B.9
  • 9
    • 0029008101 scopus 로고
    • Tetrahydrobiopterin-deficient nitric oxide synthase has a modified heme environment and forms a cytochrome P-420 analogue
    • 9 Wang, J., Stuehr, D. J. and Rousseau, D. L. (1995) Tetrahydrobiopterin-deficient nitric oxide synthase has a modified heme environment and forms a cytochrome P-420 analogue. Biochemistry 34, 7080-7087
    • (1995) Biochemistry , vol.34 , pp. 7080-7087
    • Wang, J.1    Stuehr, D.J.2    Rousseau, D.L.3
  • 10
    • 0030793667 scopus 로고    scopus 로고
    • Tetrahydrobiopterin binding to macrophage inducible nitric oxide synthase expressed in Echerichia coli. Heme spin shift and dimer stabilization by the potent pterin antagonist 4-amino tetrahydrobiopterin
    • 10 Mayer, B., Wu, C., Gorren, A. C. F., Pfeiffer, S., Schmidt, K., Clark, P., Stuehr, D. J. and Werner, E. R. (1997) Tetrahydrobiopterin binding to macrophage inducible nitric oxide synthase expressed in Echerichia coli. Heme spin shift and dimer stabilization by the potent pterin antagonist 4-amino tetrahydrobiopterin. Biochemistry 36, 8422-8427
    • (1997) Biochemistry , vol.36 , pp. 8422-8427
    • Mayer, B.1    Wu, C.2    Gorren, A.C.F.3    Pfeiffer, S.4    Schmidt, K.5    Clark, P.6    Stuehr, D.J.7    Werner, E.R.8
  • 11
    • 0030687876 scopus 로고    scopus 로고
    • Allosteric modulation of rat brain nitric oxide synthase by the pterin-site enzyme inhibitor 4-amino tetrahydrobiopterin
    • 11 Pfeiffer, S., Gorren, A. C. F., Pitters, E., Schmidt, K., Werner, E. R. and Mayer, B. (1997) Allosteric modulation of rat brain nitric oxide synthase by the pterin-site enzyme inhibitor 4-amino tetrahydrobiopterin. Biochem. J. 328, 349-352
    • (1997) Biochem. J. , vol.328 , pp. 349-352
    • Pfeiffer, S.1    Gorren, A.C.F.2    Pitters, E.3    Schmidt, K.4    Werner, E.R.5    Mayer, B.6
  • 12
    • 0030859931 scopus 로고    scopus 로고
    • The ferrousdioxy complex of neuronal nitric oxide synthase - Divergent effects of L-arginine and tetrahydrobiopterin on its stability
    • 12 Abusoud, H. M., Gachhui, R., Raushel, F. M. and Stuehr, D. J. (1997) The ferrousdioxy complex of neuronal nitric oxide synthase - divergent effects of L-arginine and tetrahydrobiopterin on its stability. J. Biol. Chem. 272, 17349-17353
    • (1997) J. Biol. Chem. , vol.272 , pp. 17349-17353
    • Abusoud, H.M.1    Gachhui, R.2    Raushel, F.M.3    Stuehr, D.J.4
  • 13
    • 0032577582 scopus 로고    scopus 로고
    • Reaction of neuronal nitric-oxide synthase with oxygen at low temperature. Evidence for reductive activation of the oxy-ferrous complex by tetrahydrobiopterin
    • 13 Bec, N., Gorren, A. C. F., Voelker, C., Mayer, B. and Lange, R. (1998) Reaction of neuronal nitric-oxide synthase with oxygen at low temperature. Evidence for reductive activation of the oxy-ferrous complex by tetrahydrobiopterin. J. Biol. Chem. 273, 13502-13508
    • (1998) J. Biol. Chem. , vol.273 , pp. 13502-13508
    • Bec, N.1    Gorren, A.C.F.2    Voelker, C.3    Mayer, B.4    Lange, R.5
  • 15
    • 0022359513 scopus 로고
    • Estimation of tetrahydro, dihydro and fully oxidised pterins by high-performance liquid chromatography using sequential electrochemical and fluorometric detection
    • 15 Hyland, K. (1985) Estimation of tetrahydro, dihydro and fully oxidised pterins by high-performance liquid chromatography using sequential electrochemical and fluorometric detection. J. Chromatogr. 343, 35-41
    • (1985) J. Chromatogr. , vol.343 , pp. 35-41
    • Hyland, K.1
  • 17
    • 0029913323 scopus 로고    scopus 로고
    • Overexpression of neuronal nitric oxide synthase in insect cells reveals requirement of haem for tetrahydrobiopterin binding
    • 17 List, B. M., Klatt, P., Werner, E. R., Schmidt, K. and Mayer, B. (1996) Overexpression of neuronal nitric oxide synthase in insect cells reveals requirement of haem for tetrahydrobiopterin binding. Biochem. J. 315, 57-63
    • (1996) Biochem. J. , vol.315 , pp. 57-63
    • List, B.M.1    Klatt, P.2    Werner, E.R.3    Schmidt, K.4    Mayer, B.5
  • 18
    • 0023082034 scopus 로고
    • Phenylalanine 4-monooxygenase from rat liver
    • 18 Kaufman, S. (1987) Phenylalanine 4-monooxygenase from rat liver. Methods Enzymol. 142, 3-17
    • (1987) Methods Enzymol. , vol.142 , pp. 3-17
    • Kaufman, S.1
  • 19
    • 0015501733 scopus 로고
    • The isolation and characterization of dihydropteridine reductase from sheep liver
    • 19 Craine, J. E., Hall, E. S. and Kaufman, S. (1972) The isolation and characterization of dihydropteridine reductase from sheep liver. J. Biol. Chem. 247, 6082-6091
    • (1972) J. Biol. Chem. , vol.247 , pp. 6082-6091
    • Craine, J.E.1    Hall, E.S.2    Kaufman, S.3
  • 20
    • 0028034105 scopus 로고
    • Molecular mechanisms of inhibition of porcine brain nitric oxide synthase by the antinociceptive drug 7-nitro-indazole
    • 20 Mayer, B., Klatt, P., Werner, E. R. and Schmidt, K. (1994) Molecular mechanisms of inhibition of porcine brain nitric oxide synthase by the antinociceptive drug 7-nitro-indazole. Neuropharmacology 33, 1253-1259
    • (1994) Neuropharmacology , vol.33 , pp. 1253-1259
    • Mayer, B.1    Klatt, P.2    Werner, E.R.3    Schmidt, K.4
  • 21
    • 0024388901 scopus 로고
    • Macrophage oxidation of L-arginine to nitric oxide, nitrite, and nitrate. Tetrahydrobiopterin is required as a cofactor
    • 21 Tayeh, M. A. and Marletta, M. A. (1989) Macrophage oxidation of L-arginine to nitric oxide, nitrite, and nitrate. Tetrahydrobiopterin is required as a cofactor. J. Biol. Chem. 264, 19654-19658
    • (1989) J. Biol. Chem. , vol.264 , pp. 19654-19658
    • Tayeh, M.A.1    Marletta, M.A.2
  • 22
    • 0025572626 scopus 로고
    • 2+/calmodulin-dependent nitric oxide synthase from porcine cerebellum. Cofactor-role of tetrahydrobiopterin
    • 2+/calmodulin-dependent nitric oxide synthase from porcine cerebellum. Cofactor-role of tetrahydrobiopterin. FEBS Lett. 277, 215-219
    • (1990) FEBS Lett. , vol.277 , pp. 215-219
    • Mayer, B.1    John, M.2    Bohme, E.3
  • 23
    • 0024385932 scopus 로고
    • Nitric oxide: Biosynthesis and biological significance
    • 23 Marletta, M. A. (1989) Nitric oxide: biosynthesis and biological significance. Trends Biochem. Sci. 14, 488-492
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 488-492
    • Marletta, M.A.1
  • 24
    • 0025848403 scopus 로고
    • Brain nitric oxide synthase is a biopterin- and flavin-containing multifunctional oxido-reductase
    • 24 Mayer, B., John, M., Heinzel, B., Werner, E. R., Wachter, H., Schultz, G. and Böhme, E. (1991) Brain nitric oxide synthase is a biopterin-and flavin-containing multifunctional oxido-reductase. FEBS Lett. 288, 187-191
    • (1991) FEBS Lett. , vol.288 , pp. 187-191
    • Mayer, B.1    John, M.2    Heinzel, B.3    Werner, E.R.4    Wachter, H.5    Schultz, G.6    Böhme, E.7
  • 25
    • 0025826860 scopus 로고
    • Tetrahydrobiopterin, a cofactor for rat cerebellar nitric oxide synthase, does not function as a reactant in the oxygenation of arginine
    • 25 Giovanelli, J., Campos, K. L. and Kaufman, S. (1991) Tetrahydrobiopterin, a cofactor for rat cerebellar nitric oxide synthase, does not function as a reactant in the oxygenation of arginine. Proc. Natl. Acad. Sci. U.S.A. 88, 7091-7095
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 7091-7095
    • Giovanelli, J.1    Campos, K.L.2    Kaufman, S.3
  • 26
    • 0025892441 scopus 로고
    • N omega-hydroxy-L-arginine is an intermediate in the biosynthesis of nitric oxide from L-arginine
    • 26 Stuehr, D. J., Kwon, N. S., Nathan, C. F., Griffith, O. W., Feldman, P. L. and Wiseman, J. (1991) N omega-hydroxy-L-arginine is an intermediate in the biosynthesis of nitric oxide from L-arginine. J. Biol. Chem. 266, 6259-6263
    • (1991) J. Biol. Chem. , vol.266 , pp. 6259-6263
    • Stuehr, D.J.1    Kwon, N.S.2    Nathan, C.F.3    Griffith, O.W.4    Feldman, P.L.5    Wiseman, J.6
  • 28
    • 0032416666 scopus 로고    scopus 로고
    • Crystal structure of constitutive endothelial nitric oxide synthase: A paradigm for pterin function involving a novel metal center
    • 28 Raman, C. S., Li, H., Martasek, P., Kral, V., Masters, B. S. and Poulos, T. (1998) Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center. Cell 95, 939-950
    • (1998) Cell , vol.95 , pp. 939-950
    • Raman, C.S.1    Li, H.2    Martasek, P.3    Kral, V.4    Masters, B.S.5    Poulos, T.6
  • 29
    • 0033553802 scopus 로고    scopus 로고
    • Chemical puzzles posed by a biological messenger
    • 29 Pfeiffer, S., Mayer, B. and Hemmens, B. (1999) Chemical puzzles posed by a biological messenger. Angew. Chem. Int. Ed. 38, 1714-1731
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1714-1731
    • Pfeiffer, S.1    Mayer, B.2    Hemmens, B.3
  • 30
    • 0033619713 scopus 로고    scopus 로고
    • Formation of a pterin radical in the reaction of the heme domain of inducible nitric oxide synthase with oxygen
    • 30 Hurshman, A. R., Krebs, C., Edmondson, D. E., Huynh, B. H. and Marletta, M. A. (1999) Formation of a pterin radical in the reaction of the heme domain of inducible nitric oxide synthase with oxygen. Biochemistry 38, 15689-15696
    • (1999) Biochemistry , vol.38 , pp. 15689-15696
    • Hurshman, A.R.1    Krebs, C.2    Edmondson, D.E.3    Huynh, B.H.4    Marletta, M.A.5
  • 33
    • 0032719403 scopus 로고    scopus 로고
    • Electronic structure of tetrahydropteridine derivatives
    • 33 Reibnegger G., Pauschenwein J. and Werner, E. R. (1999) Electronic structure of tetrahydropteridine derivatives. Pteridines 10, 91-94
    • (1999) Pteridines , vol.10 , pp. 91-94
    • Reibnegger, G.1    Pauschenwein, J.2    Werner, E.R.3


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