메뉴 건너뛰기




Volumn 18, Issue 5, 1999, Pages 397-407

Chimeric forms of neuronal nitric oxide synthase identify different regions of the reductase domain that are essential for dimerization and activity

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CHIMERIC PROTEIN; CITRULLINE; CYTOCHROME P450 REDUCTASE; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0032997656     PISSN: 10445498     EISSN: None     Source Type: Journal    
DOI: 10.1089/104454999315286     Document Type: Article
Times cited : (8)

References (37)
  • 1
    • 0029935269 scopus 로고    scopus 로고
    • Intracellular assembly of inducible NO synthase is limited by nitric oxide-mediated changes in heme insertion and availability
    • ALBAKRI, Q.A., and STUEHR, D.J. (1996). Intracellular assembly of inducible NO synthase is limited by nitric oxide-mediated changes in heme insertion and availability. J. Biol. Chem. 271, 5414-5421.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5414-5421
    • Albakri, Q.A.1    Stuehr, D.J.2
  • 2
    • 0025350086 scopus 로고
    • An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusion
    • ARGOS, P. (1990). An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusion. J. Mol. Biol. 211, 943-958.
    • (1990) J. Mol. Biol. , vol.211 , pp. 943-958
    • Argos, P.1
  • 3
    • 0028284568 scopus 로고
    • The mitochondrial environment is required for activity of the cholesterol side-chain cleavage enzyme, cytochrome P450scc
    • BLACK, S.M., HARIKRISHNA, J.A., SZLARZ, G.D., and MILLER, W.L. (1994). The mitochondrial environment is required for activity of the cholesterol side-chain cleavage enzyme, cytochrome P450scc. Proc. Natl. Acad. Sci. USA 91, 7247-7251.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7247-7251
    • Black, S.M.1    Harikrishna, J.A.2    Szlarz, G.D.3    Miller, W.L.4
  • 4
    • 0029056135 scopus 로고
    • Characterization of rat neuronal nitric oxide synthase expressed in Saccharomyces cerevisiae
    • BLACK, S.M., and ORTIZ DE MONTELLANO, P.R. (1995). Characterization of rat neuronal nitric oxide synthase expressed in Saccharomyces cerevisiae. DNA Cell Biol. 14, 789-794.
    • (1995) DNA Cell Biol. , vol.14 , pp. 789-794
    • Black, S.M.1    Ortiz De Montellano, P.R.2
  • 5
    • 0027398066 scopus 로고
    • Regulation of proteins in the cholesterol side-chain cleavage system in JEG-3 and Y-1 cells
    • BLACK, S.M., SZLARZ, G.D., HARIKRISHNA, J.A., LIN, D., WOLF, C.R., and MILLER, W.L. (1993). Regulation of proteins in the cholesterol side-chain cleavage system in JEG-3 and Y-1 cells. Endocrinology 132, 539-545.
    • (1993) Endocrinology , vol.132 , pp. 539-545
    • Black, S.M.1    Szlarz, G.D.2    Harikrishna, J.A.3    Lin, D.4    Wolf, C.R.5    Miller, W.L.6
  • 6
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • BREDT, D.S., HWANG, P.M., GLATT, C.E., LOWENSTEIN, C., REED, R.R., and SNYDER, S.H. (1991). Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature 351, 714-718.
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5    Snyder, S.H.6
  • 7
    • 0026731333 scopus 로고
    • Biosynthesis of nitric oxide and citrulline from L-arginine by constitutive nitric oxide synthase present in rabbit corpus cavernosum
    • BUSH, P.A., GONZALEZ, N.E., and IGNARRO, L.J. (1992). Biosynthesis of nitric oxide and citrulline from L-arginine by constitutive nitric oxide synthase present in rabbit corpus cavernosum. Biochem. Biophys. Res. Commun. 186, 308-314.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 308-314
    • Bush, P.A.1    Gonzalez, N.E.2    Ignarro, L.J.3
  • 8
    • 0029558027 scopus 로고
    • Inducible nitric oxide synthase: Identification of amino acid residues essential for dimerization and binding of tetrahydrobiopterin
    • CHO, H.J., MARTIN, E., XIE, Q.W., SASSA, S., and NATHAN, C. (1995). Inducible nitric oxide synthase: identification of amino acid residues essential for dimerization and binding of tetrahydrobiopterin. Proc. Natl. Acad. Sci. USA 92, 11514-11518.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11514-11518
    • Cho, H.J.1    Martin, E.2    Xie, Q.W.3    Sassa, S.4    Nathan, C.5
  • 9
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • CHOMCZYNSKI, P., and SACCHI, N. (1987). Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 11
    • 0029848531 scopus 로고    scopus 로고
    • Construction of a P450c27 fusion enzyme: A useful tool for analysis of vitamin D-3 25-hydroxylase activity
    • DILWORTH, F.J., BLACK, S.M., GUO, Y.D., MILLER, W.L., and JONES, G. (1996). Construction of a P450c27 fusion enzyme: a useful tool for analysis of vitamin D-3 25-hydroxylase activity. Biochem. J. 320, 267-271.
    • (1996) Biochem. J. , vol.320 , pp. 267-271
    • Dilworth, F.J.1    Black, S.M.2    Guo, Y.D.3    Miller, W.L.4    Jones, G.5
  • 12
    • 0025922972 scopus 로고
    • P450bm-3 and other inducible bacterial P450 cytochromes: Biochemistry and regulation
    • FULCO, A.J. (1991). P450bm-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation. Annu. Rev. Pharmacol. Toxicol. 31, 177-203.
    • (1991) Annu. Rev. Pharmacol. Toxicol. , vol.31 , pp. 177-203
    • Fulco, A.J.1
  • 14
    • 0030758321 scopus 로고    scopus 로고
    • Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction
    • GHOSH, D.K., WU, C.Q., PITTERS, E., MOLONEY, M., WERNER, E.R., MAYER, B., and STUEHR, D.J. (1997). Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction. Biochemistry 36, 10609-10619.
    • (1997) Biochemistry , vol.36 , pp. 10609-10619
    • Ghosh, D.K.1    Wu, C.Q.2    Pitters, E.3    Moloney, M.4    Werner, E.R.5    Mayer, B.6    Stuehr, D.J.7
  • 15
    • 0027311918 scopus 로고
    • Construction and function of fusion enzymes of the human cytochrome-P450scc system
    • HARIKRISHNA, J.A.. BLACK, S.M., D., S.G., and MILLER, W.L. (1993). Construction and function of fusion enzymes of the human cytochrome-P450scc system. DNA Cell Biol. 12, 371-379.
    • (1993) DNA Cell Biol. , vol.12 , pp. 371-379
    • Harikrishna, J.A.1    Black, S.M.2    D., S.G.3    Miller, W.L.4
  • 16
    • 0027500278 scopus 로고
    • Basal transcriptional activity and cyclic adenosine 3′,5′-monophosphate responsiveness of the human cytochrome-P450scc promoter transfected into MA-10 Leydig cells
    • HUM, D.W., STAELS, B., BLACK, S.M., and MILLER, W.L. (1993). Basal transcriptional activity and cyclic adenosine 3′,5′-monophosphate responsiveness of the human cytochrome-P450scc promoter transfected into MA-10 Leydig cells. Endocrinology 132, 546-552.
    • (1993) Endocrinology , vol.132 , pp. 546-552
    • Hum, D.W.1    Staels, B.2    Black, S.M.3    Miller, W.L.4
  • 17
    • 0025321355 scopus 로고
    • Biosynthesis and metabolism of endothelium-derived nitric oxide
    • IGNARRO, L.J. (1990). Biosynthesis and metabolism of endothelium-derived nitric oxide. Annu. Rev. Pharmacol. Toxicol. 30, 535-560.
    • (1990) Annu. Rev. Pharmacol. Toxicol. , vol.30 , pp. 535-560
    • Ignarro, L.J.1
  • 18
    • 0026023225 scopus 로고
    • + reductase: Prototype for a structurally novel flavoenzyme family
    • + reductase: prototype for a structurally novel flavoenzyme family. Science 251, 60-66.
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 19
    • 0026687419 scopus 로고
    • Stimulation of human nitric oxide synthase by tetrahydrobiopterin and selective binding of the cofactor
    • KLATT, P., HEIZEL, B., MAYER, B., AMBACH, E., WERNERFELMAYER, G., WACHTER, H., and WERNER, E.R. (1992a). Stimulation of human nitric oxide synthase by tetrahydrobiopterin and selective binding of the cofactor. FEBS Lett. 305, 160-162.
    • (1992) FEBS Lett. , vol.305 , pp. 160-162
    • Klatt, P.1    Heizel, B.2    Mayer, B.3    Ambach, E.4    Wernerfelmayer, G.5    Wachter, H.6    Werner, E.R.7
  • 20
    • 0029929385 scopus 로고    scopus 로고
    • Characterization of heme-deficient neuronal nitric-oxide synthase reveals a role for heme in subunit dimerization and binding of the amino acid substrate and tetrahydrobiopterin
    • KLATT, P., PFEIFFER, S., LIST, B.M., LEHNER, D., GLATTER, O., BACHINGER, H.P., WERNER, E.R., SCHMIDT, K., and MAYER, B. (1996). Characterization of heme-deficient neuronal nitric-oxide synthase reveals a role for heme in subunit dimerization and binding of the amino acid substrate and tetrahydrobiopterin. J. Biol. Chem. 271, 7336-7342.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7336-7342
    • Klatt, P.1    Pfeiffer, S.2    List, B.M.3    Lehner, D.4    Glatter, O.5    Bachinger, H.P.6    Werner, E.R.7    Schmidt, K.8    Mayer, B.9
  • 21
    • 0026437792 scopus 로고
    • Brain nitric oxide synthase is a haemoprotein
    • KLATT, P., SCHMIDT, K., and MAYER, B. (1992b). Brain nitric oxide synthase is a haemoprotein. Biochem. J. 288, 15-17.
    • (1992) Biochem. J. , vol.288 , pp. 15-17
    • Klatt, P.1    Schmidt, K.2    Mayer, B.3
  • 22
    • 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
    • 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
  • 23
    • 0026623110 scopus 로고
    • Endothelial nitric oxide synthase: Molecular cloning and characterization of a distinct constitutive enzyme isoform
    • LAMAS, S., MARSDEN, P.A., LI, G.K., TEMPST, P., and MICHEL, T. (1992). Endothelial nitric oxide synthase: molecular cloning and characterization of a distinct constitutive enzyme isoform. Proc. Natl. Acad. Sci. USA 89, 6348-6352.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6348-6352
    • Lamas, S.1    Marsden, P.A.2    Li, G.K.3    Tempst, P.4    Michel, T.5
  • 24
    • 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
    • LIST, B.M., KLOSCH, B., VOLKER, C., GORREN, A.C.F., SESSA, W.C., WERNER, E.R., KUKOVETZ, 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.F.4    Sessa, W.C.5    Werner, E.R.6    Kukovetz, W.R.7    Schmidt, K.8    Mayer, B.9
  • 25
    • 0026729267 scopus 로고
    • Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme
    • LOWENSTEIN, C.J., GLATT, C.S., BREDT, D.S., and SNYDER, S.H. (1992). Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme. Proc. Natl. Acad. Sci. USA 89, 6711-6715.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6711-6715
    • Lowenstein, C.J.1    Glatt, C.S.2    Bredt, D.S.3    Snyder, S.H.4
  • 27
    • 0025848403 scopus 로고
    • Brain nitric oxide synthase is a biopterin-containing and flavin-containing multi-functional oxido-reductase
    • MAYER, B., JOHN, M., HEINZEL, B., WERNER, E.R., WACHTER, H., SCHULTZ, G., and BOHME, E. (1991). Brain nitric oxide synthase is a biopterin-containing and flavin-containing multi-functional 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    Bohme, E.7
  • 28
    • 0025784834 scopus 로고
    • Endogenous nitric oxide: Physiology, pathology and clinical relevance
    • MONCADA, S., and HIGGS, E.A. (1991). Endogenous nitric oxide: physiology, pathology and clinical relevance. Eur. J. Clin. Invest. 21, 361-374.
    • (1991) Eur. J. Clin. Invest. , vol.21 , pp. 361-374
    • Moncada, S.1    Higgs, E.A.2
  • 31
    • 0025695687 scopus 로고
    • Dexamethasone prevents the induction by endotoxin of a nitric oxide synthase and the associated effects on vascular tone: An insight into endotoxin shock
    • REES, D.D., CELLEK, S., PALMER, R.M.J., and MONCADA, S. (1990). Dexamethasone prevents the induction by endotoxin of a nitric oxide synthase and the associated effects on vascular tone: an insight into endotoxin shock. Biochem. Biophys. Res. Commun. 173, 541-547.
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 541-547
    • Rees, D.D.1    Cellek, S.2    Palmer, R.M.J.3    Moncada, S.4
  • 32
    • 0029889353 scopus 로고    scopus 로고
    • Endothelial nitric-oxide synthase: Expression in Escherichia coli, spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation
    • RODRIGUEZ-CRESPO, I., GERBER, N.C., and ORTIZ DE MONTELLANO, P.R. (1996). Endothelial nitric-oxide synthase: expression in Escherichia coli, spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation. J. Biol. Chem. 271, 11462-11467.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11462-11467
    • Rodriguez-Crespo, I.1    Gerber, N.C.2    Ortiz De Montellano, P.R.3
  • 33
    • 0030446051 scopus 로고    scopus 로고
    • Human endothelial nitric oxide synthase: Expression in Escherichia coli, coexpression with calmodulin, and characterization
    • RODRIGUEZ-CRESPO, I., and ORTIZ DE MONTELLANO, P.R. (1996). Human endothelial nitric oxide synthase: expression in Escherichia coli, coexpression with calmodulin, and characterization. Arch. Biochem. Biophys. 336, 151-156.
    • (1996) Arch. Biochem. Biophys. , vol.336 , pp. 151-156
    • Rodriguez-Crespo, I.1    Ortiz De Montellano, P.R.2
  • 34
    • 0025962972 scopus 로고
    • Nitric oxide as a neuronal messenger
    • SNYDER, S.H., and BREDT, D.S. (1991). Nitric oxide as a neuronal messenger. Trends Pharmacol. Sci. 12, 125-128.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 125-128
    • Snyder, S.H.1    Bredt, D.S.2
  • 35
    • 0027426441 scopus 로고
    • Increased levels of alpha-class and pi-class glutathione Stransferases in cell lines resistant to 1-chloro-2,4-dinitrobenzene
    • WAREING, C.J., BLACK, S.M., HAYES, J.D., and WOLF, C.R. (1993). Increased levels of alpha-class and pi-class glutathione Stransferases in cell lines resistant to 1-chloro-2,4-dinitrobenzene. Eur. J. Biochem. 217, 671-676.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 671-676
    • Wareing, C.J.1    Black, S.M.2    Hayes, J.D.3    Wolf, C.R.4
  • 37
    • 0028097287 scopus 로고
    • Carboxyl terminus of inducible nitric oxide synthase: Contribution to NADPH binding and enzymatic activity
    • XIE, Q.W., CHO, H., KASHIWABARA, Y., BAUM, M., WEIDNER, J.R., ELLISTON, K., MUMFORD, R., and NATHAN, C. (1994). Carboxyl terminus of inducible nitric oxide synthase: contribution to NADPH binding and enzymatic activity. J. Biol. Chem. 269, 28500-28505.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28500-28505
    • Xie, Q.W.1    Cho, H.2    Kashiwabara, Y.3    Baum, M.4    Weidner, J.R.5    Elliston, K.6    Mumford, R.7    Nathan, C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.