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Volumn 87, Issue 3 SPEC. ISS., 2006, Pages 226-232

Biochemical properties of recombinant human and mouse N-acetylglutamate synthase

Author keywords

Acetylglutamate; Arginine; Hyperammonemia; Urea cycle; Ureagenesis

Indexed keywords

ARGININE; GLUTAMATE ACETYLTRANSFERASE; N ACETYLGLUTAMIC ACID; RECOMBINANT ENZYME;

EID: 33644647181     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2005.10.003     Document Type: Article
Times cited : (30)

References (36)
  • 1
    • 0038485942 scopus 로고    scopus 로고
    • Null mutations in the N-acetylglutamate synthase gene associated with acute neonatal disease and hyperammonemia
    • L. Caldovic, H. Morizono, M.G. Panglao, S.F. Cheng, S. Packman, and M. Tuchman Null mutations in the N-acetylglutamate synthase gene associated with acute neonatal disease and hyperammonemia Hum. Genet. 112 2003 364 368
    • (2003) Hum. Genet. , vol.112 , pp. 364-368
    • Caldovic, L.1    Morizono, H.2    Panglao, M.G.3    Cheng, S.F.4    Packman, S.5    Tuchman, M.6
  • 3
    • 0036894166 scopus 로고    scopus 로고
    • N-Acetylglutamate synthase deficiency and the treatment of hyperammonemic encephalopathy
    • O. Elpeleg, A. Shaag, E. Ben-Shalom, T. Schmid, and C. Bachmann N-Acetylglutamate synthase deficiency and the treatment of hyperammonemic encephalopathy Ann. Neurol. 52 2002 845 849
    • (2002) Ann. Neurol. , vol.52 , pp. 845-849
    • Elpeleg, O.1    Shaag, A.2    Ben-Shalom, E.3    Schmid, T.4    Bachmann, C.5
  • 5
    • 18844453488 scopus 로고    scopus 로고
    • Identification of novel mutations of the human N-acetylglutamate synthase gene and their functional investigation by expression studies
    • E. Schmidt, J.M. Nuoffer, J. Haberle, S. Pauli, N. Guffon, C. Vianey-Saban, B. Wermuth, and H.G. Koch Identification of novel mutations of the human N-acetylglutamate synthase gene and their functional investigation by expression studies Biochim. Biophys. Acta 1740 2005 54 59
    • (2005) Biochim. Biophys. Acta , vol.1740 , pp. 54-59
    • Schmidt, E.1    Nuoffer, J.M.2    Haberle, J.3    Pauli, S.4    Guffon, N.5    Vianey-Saban, C.6    Wermuth, B.7    Koch, H.G.8
  • 7
    • 0017854128 scopus 로고
    • N-Acetylglutamate synthetase from rat-liver mitochondria. Partial purification and catalytic properties
    • K. Shigesada, and M. Tatibana N-Acetylglutamate synthetase from rat-liver mitochondria. Partial purification and catalytic properties Eur. J. Biochem. 84 1978 285 291
    • (1978) Eur. J. Biochem. , vol.84 , pp. 285-291
    • Shigesada, K.1    Tatibana, M.2
  • 8
    • 0021112506 scopus 로고
    • Purification of N-acetyl-l-glutamate synthetase from rat liver mitochondria and substrate and activator specificity of the enzyme
    • T. Sonoda, and M. Tatibana Purification of N-acetyl-l-glutamate synthetase from rat liver mitochondria and substrate and activator specificity of the enzyme J. Biol. Chem. 258 1983 9839 9844
    • (1983) J. Biol. Chem. , vol.258 , pp. 9839-9844
    • Sonoda, T.1    Tatibana, M.2
  • 9
    • 0019574036 scopus 로고
    • Subcellular localization and properties of N-acetylglutamate synthase in rat small intestinal mucosa
    • C. Uchiyama, M. Mori, and M. Tatibana Subcellular localization and properties of N-acetylglutamate synthase in rat small intestinal mucosa J. Biochem. (Tokyo) 89 1981 1777 1786
    • (1981) J. Biochem. (Tokyo) , vol.89 , pp. 1777-1786
    • Uchiyama, C.1    Mori, M.2    Tatibana, M.3
  • 10
    • 0020164721 scopus 로고
    • Purification and properties of acetyl-CoA:l-glutamate N-acetyltransferase from human liver
    • C. Bachmann, S. Krahenbuhl, and J.P. Colombo Purification and properties of acetyl-CoA:l-glutamate N-acetyltransferase from human liver Biochem. J. 205 1982 123 127
    • (1982) Biochem. J. , vol.205 , pp. 123-127
    • Bachmann, C.1    Krahenbuhl, S.2    Colombo, J.P.3
  • 13
    • 0002478552 scopus 로고
    • Regulation of urea biosynthesis by the acetylglutamate-arginine system
    • S. Grisolia R. Baguena F. Mayor John Wiley New York
    • M. Tatibana, and K. Shigesada Regulation of urea biosynthesis by the acetylglutamate-arginine system S. Grisolia R. Baguena F. Mayor The Urea Cycle 1976 John Wiley New York 301 315
    • (1976) The Urea Cycle , pp. 301-315
    • Tatibana, M.1    Shigesada, K.2
  • 14
    • 0025852726 scopus 로고
    • Control of urea synthesis and ammonia utilization in protein deprivation and refeeding
    • V. Felipo, M.D. Minana, and S. Grisolia Control of urea synthesis and ammonia utilization in protein deprivation and refeeding Arch. Biochem. Biophys. 285 1991 351 356
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 351-356
    • Felipo, V.1    Minana, M.D.2    Grisolia, S.3
  • 15
    • 0017687409 scopus 로고
    • Regulation of urea synthesis in rat liver. Changes of ornithine and acetylglutamate concentrations in the livers of rats subjected to dietary transitions
    • T. Saheki, T. Katsunuma, and M. Sase Regulation of urea synthesis in rat liver. Changes of ornithine and acetylglutamate concentrations in the livers of rats subjected to dietary transitions J. Biochem. (Tokyo) 82 1977 551 558
    • (1977) J. Biochem. (Tokyo) , vol.82 , pp. 551-558
    • Saheki, T.1    Katsunuma, T.2    Sase, M.3
  • 16
    • 0015119192 scopus 로고
    • Enzymatic synthesis of acetylglutamate by mammalian liver preparations and its stimulation by arginine
    • K. Shigesada, and M. Tatibana Enzymatic synthesis of acetylglutamate by mammalian liver preparations and its stimulation by arginine Biochem. Biophys. Res. Commun. 44 1971 1117 1124
    • (1971) Biochem. Biophys. Res. Commun. , vol.44 , pp. 1117-1124
    • Shigesada, K.1    Tatibana, M.2
  • 17
    • 0020349936 scopus 로고
    • Regulation of the N-acetylglutamate content of rat hepatocytes by the glutamate concentration
    • H. Zollner Regulation of the N-acetylglutamate content of rat hepatocytes by the glutamate concentration Adv. Exp. Med. Biol. 153 1982 197 205
    • (1982) Adv. Exp. Med. Biol. , vol.153 , pp. 197-205
    • Zollner, H.1
  • 18
    • 0017810934 scopus 로고
    • Role of acetylglutamate in ureotelism. Variations in acetylglutamate level and its possible significance in control of urea synthesis in mammalian liver
    • K. Shigesada, K. Aoyagi, and M. Tatibana Role of acetylglutamate in ureotelism. Variations in acetylglutamate level and its possible significance in control of urea synthesis in mammalian liver Eur. J. Biochem. 85 1978 385 391
    • (1978) Eur. J. Biochem. , vol.85 , pp. 385-391
    • Shigesada, K.1    Aoyagi, K.2    Tatibana, M.3
  • 19
    • 0018968098 scopus 로고
    • Short term regulation of ureagenesis
    • P.M. Stewart, and M. Walser Short term regulation of ureagenesis J. Biol. Chem. 255 1980 5270 5280
    • (1980) J. Biol. Chem. , vol.255 , pp. 5270-5280
    • Stewart, P.M.1    Walser, M.2
  • 20
    • 0025630487 scopus 로고
    • Effect of level of dietary protein on arginine-stimulated citrulline synthesis. Correlation with mitochondrial N-acetylglutamate concentrations
    • B.H. Morimoto, J.F. Brady, and D.E. Atkinson Effect of level of dietary protein on arginine-stimulated citrulline synthesis. Correlation with mitochondrial N-acetylglutamate concentrations Biochem. J. 272 1990 671 675
    • (1990) Biochem. J. , vol.272 , pp. 671-675
    • Morimoto, B.H.1    Brady, J.F.2    Atkinson, D.E.3
  • 21
    • 0020028835 scopus 로고
    • Regulation of N-acetylglutamate synthetase in mouse liver. Postprandial changes in sensitivity to activation by arginine
    • S. Kawamoto, H. Ishida, M. Mori, and M. Tatibana Regulation of N-acetylglutamate synthetase in mouse liver. Postprandial changes in sensitivity to activation by arginine Eur. J. Biochem. 123 1982 637 641
    • (1982) Eur. J. Biochem. , vol.123 , pp. 637-641
    • Kawamoto, S.1    Ishida, H.2    Mori, M.3    Tatibana, M.4
  • 22
    • 0020388931 scopus 로고
    • Enzyme regulation of N-acetylglutamate synthesis in mouse and rat liver
    • M. Tatibana, S. Kawamoto, T. Sonoda, and M. Mori Enzyme regulation of N-acetylglutamate synthesis in mouse and rat liver Adv. Exp. Med. Biol. 153 1982 207 216
    • (1982) Adv. Exp. Med. Biol. , vol.153 , pp. 207-216
    • Tatibana, M.1    Kawamoto, S.2    Sonoda, T.3    Mori, M.4
  • 23
    • 0021360498 scopus 로고
    • Is N-acetylglutamate a short-term regulator of urea synthesis
    • P. Lund, and D. Wiggins Is N-acetylglutamate a short-term regulator of urea synthesis Biochem. J. 218 1984 991 994
    • (1984) Biochem. J. , vol.218 , pp. 991-994
    • Lund, P.1    Wiggins, D.2
  • 24
    • 0021127291 scopus 로고
    • N-Acetylglutamate in rat liver during foetal development
    • M. Van Dijk, and P. Lund N-Acetylglutamate in rat liver during foetal development Biochem. J. 222 1984 837 838
    • (1984) Biochem. J. , vol.222 , pp. 837-838
    • Van Dijk, M.1    Lund, P.2
  • 27
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
    • P. Sheffield, S. Garrard, and Z. Derewenda Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors Protein. Expr. Purif. 15 1999 34 39
    • (1999) Protein. Expr. Purif. , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 28
    • 0017645827 scopus 로고
    • Effect of glucagon on metabolite compartmentation in isolated rat liver cells during gluconeogenesis from lactate
    • E.A. Siess, D.G. Brocks, H.K. Lattke, and O.H. Wieland Effect of glucagon on metabolite compartmentation in isolated rat liver cells during gluconeogenesis from lactate Biochem. J. 166 1977 225 235
    • (1977) Biochem. J. , vol.166 , pp. 225-235
    • Siess, E.A.1    Brocks, D.G.2    Lattke, H.K.3    Wieland, O.H.4
  • 29
    • 0017194459 scopus 로고
    • Subcellular distribution of key metabolites in isolated liver cells from fasted rats
    • E.A. Siess, D.G. Brocks, and O.H. Wieland Subcellular distribution of key metabolites in isolated liver cells from fasted rats FEBS Lett. 69 1976 265 271
    • (1976) FEBS Lett. , vol.69 , pp. 265-271
    • Siess, E.A.1    Brocks, D.G.2    Wieland, O.H.3
  • 30
    • 0022339822 scopus 로고
    • Modulation of the activity of rat liver acetylglutamate synthase by pH and arginine concentration
    • E.S. Kamemoto, and D.E. Atkinson Modulation of the activity of rat liver acetylglutamate synthase by pH and arginine concentration Arch. Biochem. Biophys. 243 1985 100 107
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 100-107
    • Kamemoto, E.S.1    Atkinson, D.E.2
  • 31
    • 0021824384 scopus 로고
    • Nutritional influences on the distribution of the urea cycle: Intermediates in isolated hepatocytes
    • R.A. Freedland, A.J. Meijer, and J.M. Tager Nutritional influences on the distribution of the urea cycle: intermediates in isolated hepatocytes Fed. Proc. 44 1985 2453 2457
    • (1985) Fed. Proc. , vol.44 , pp. 2453-2457
    • Freedland, R.A.1    Meijer, A.J.2    Tager, J.M.3
  • 34
    • 0022349399 scopus 로고
    • Stimulatory effect of arginine on acetylglutamate synthesis in isolated mitochondria of mouse and rat liver
    • S. Kawamoto, T. Sonoda, A. Ohtake, and M. Tatibana Stimulatory effect of arginine on acetylglutamate synthesis in isolated mitochondria of mouse and rat liver Biochem. J. 232 1985 329 334
    • (1985) Biochem. J. , vol.232 , pp. 329-334
    • Kawamoto, S.1    Sonoda, T.2    Ohtake, A.3    Tatibana, M.4
  • 35
    • 0038000608 scopus 로고    scopus 로고
    • N-Acetylglutamate and its changing role through evolution
    • L. Caldovic, and M. Tuchman N-Acetylglutamate and its changing role through evolution Biochem. J. 372 2003 279 290
    • (2003) Biochem. J. , vol.372 , pp. 279-290
    • Caldovic, L.1    Tuchman, M.2
  • 36
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell. Biol. 6 2005 197 208
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2


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