메뉴 건너뛰기




Volumn 81, Issue SUPPL., 2004, Pages 4-11

Mammalian N-acetylglutamate synthase

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A; ACYLTRANSFERASE; AMINO ACID; CARBAMATE KINASE; CARBAMOYL PHOSPHATE SYNTHASE; CARGLUMIC ACID; GLUTAMATE ACETYLTRANSFERASE; GLUTAMIC ACID DERIVATIVE; N CARBAMYLGLUTAMATE; UNCLASSIFIED DRUG;

EID: 1642465569     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ymgme.2003.10.017     Document Type: Article
Times cited : (38)

References (38)
  • 1
    • 0003289912 scopus 로고
    • Catalytic role of glutamate derivatives in citrulline biosynthesis
    • Grisolia S., Cohen P.P. Catalytic role of glutamate derivatives in citrulline biosynthesis. J. Biol. Chem. 204:1953;753-757.
    • (1953) J. Biol. Chem. , vol.204 , pp. 753-757
    • Grisolia, S.1    Cohen, P.P.2
  • 2
    • 70449226017 scopus 로고
    • Purification of carbamyl phosphate synthetase from frog liver
    • Marshall M., Metzenberg R.L., Cohen P.P. Purification of carbamyl phosphate synthetase from frog liver. J. Biol. Chem. 233:1958;102-105.
    • (1958) J. Biol. Chem. , vol.233 , pp. 102-105
    • Marshall, M.1    Metzenberg, R.L.2    Cohen, P.P.3
  • 3
    • 0015119192 scopus 로고
    • Enzymatic synthesis of acetylglutamate by mammalian liver preparations and its stimulation by arginine
    • Shigesada K., Tatibana M. 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
  • 5
    • 0037021613 scopus 로고    scopus 로고
    • Role of N -acetylglutamate concentration and ornithine transport into mitochondria in urea synthesis of rats given proteins of different quality
    • Tujioka K., Lyou K.S., Hirano E., Sano A., Hayase K., Yoshida A., Yokogoshi H. Role of. N -acetylglutamate concentration and ornithine transport into mitochondria in urea synthesis of rats given proteins of different quality J. Agric. Food Chem. 50:2002;7467-7471.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 7467-7471
    • Tujioka, K.1    Lyou, K.S.2    Hirano, E.3    Sano, A.4    Hayase, K.5    Yoshida, A.6    Yokogoshi, H.7
  • 6
    • 0020392133 scopus 로고
    • N -Acetylglutamate synthetase (NAGS) deficiency: Diagnosis, clinical observations and treatment
    • Bachmann C., Colombo J.P., Jaggi K. N -Acetylglutamate synthetase (NAGS) deficiency: diagnosis, clinical observations and treatment Adv. Exp. Med. Biol. 153:1982;39-45.
    • (1982) Adv. Exp. Med. Biol. , vol.153 , pp. 39-45
    • Bachmann, C.1    Colombo, J.P.2    Jaggi, K.3
  • 7
    • 0020164721 scopus 로고
    • Purification and properties of acetyl-CoA: L-glutamate N -acetyltransferase from human liver
    • Bachmann C., Krahenbuhl S., Colombo J.P. 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
  • 8
    • 0017854128 scopus 로고
    • N -Acetylglutamate synthetase from rat-liver mitochondria. Partial purification and catalytic properties
    • Shigesada K., Tatibana M. 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
  • 9
    • 0021112506 scopus 로고
    • Purification of N -acetyl-L-glutamate synthetase from rat liver mitochondria and substrate and activator specificity of the enzyme
    • Sonoda T., Tatibana M. 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
  • 10
    • 0016527085 scopus 로고
    • Organization and control in the arginine biosynthetic pathway of Neurospora
    • Cybis J., Davis R.H. Organization and control in the arginine biosynthetic pathway of Neurospora. J. Bacteriol. 123:1975;196-202.
    • (1975) J. Bacteriol. , vol.123 , pp. 196-202
    • Cybis, J.1    Davis, R.H.2
  • 11
    • 0018131294 scopus 로고
    • Arginine metabolism in Saccharomyces cerevisiae: Subcellular localization of the enzymes
    • Jauniaux J.C., Urrestarazu L.A., Wiame J.M. Arginine metabolism in Saccharomyces cerevisiae: subcellular localization of the enzymes. J. Bacteriol. 133:1978;1096-1107.
    • (1978) J. Bacteriol. , vol.133 , pp. 1096-1107
    • Jauniaux, J.C.1    Urrestarazu, L.A.2    Wiame, J.M.3
  • 13
    • 0038485942 scopus 로고    scopus 로고
    • Null mutations in the N -acetylglutamate synthase gene associated with acute neonatal disease and hyperammonemia
    • Caldovic L., Morizono H., Panglao M.G., Cheng S.F., Packman S., Tuchman M. 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
  • 15
    • 0038000608 scopus 로고    scopus 로고
    • N -Acetylglutamate and its changing role through evolution
    • Caldovic L., Tuchman M. 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
  • 16
    • 0242696523 scopus 로고    scopus 로고
    • Acetylglutamate synthase from Neurospora crassa: Structure and regulation of expression
    • Yu Y.G., Turner G.E., Weiss R.L. Acetylglutamate synthase from Neurospora crassa: structure and regulation of expression. Mol. Microbiol. 22:1996;545-554.
    • (1996) Mol. Microbiol. , vol.22 , pp. 545-554
    • Yu, Y.G.1    Turner, G.E.2    Weiss, R.L.3
  • 18
    • 0033619787 scopus 로고    scopus 로고
    • Mitochondrial processing peptidase: Multiple-site recognition of precursor proteins
    • Ito A. Mitochondrial processing peptidase: multiple-site recognition of precursor proteins. Biochem. Biophys. Res. Commun. 265:1999;611-616.
    • (1999) Biochem. Biophys. Res. Commun. , vol.265 , pp. 611-616
    • Ito, A.1
  • 19
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annu. Rev. Biochem. 66:1997;863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 20
    • 0035798406 scopus 로고    scopus 로고
    • Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure
    • Gough J., Karplus K., Hughey R., Chothia C. Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure. J. Mol. Biol. 313:2001;903-919.
    • (2001) J. Mol. Biol. , vol.313 , pp. 903-919
    • Gough, J.1    Karplus, K.2    Hughey, R.3    Chothia, C.4
  • 22
    • 0036118398 scopus 로고    scopus 로고
    • Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis
    • Ramon-Maiques S., Marina A., Gil-Ortiz F., Fita I., Rubio V. Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis. Structure. 10:2002;329-342.
    • (2002) Structure , vol.10 , pp. 329-342
    • Ramon-Maiques, S.1    Marina, A.2    Gil-Ortiz, F.3    Fita, I.4    Rubio, V.5
  • 23
    • 0033168714 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme a
    • Clements A., Rojas J.R., Trievel R.C., Wang L., Berger S.L., Marmorstein R. Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A. EMBO J. 18:1999;3521-3532.
    • (1999) EMBO J. , vol.18 , pp. 3521-3532
    • Clements, A.1    Rojas, J.R.2    Trievel, R.C.3    Wang, L.4    Berger, S.L.5    Marmorstein, R.6
  • 25
    • 0025123436 scopus 로고
    • Human hepatic N -acetylglutamate content and N -acetylglutamate synthase activity. Determination by stable isotope dilution
    • Tuchman M., Holzknecht R.A. Human hepatic. N -acetylglutamate content and N -acetylglutamate synthase activity. Determination by stable isotope dilution Biochem. J. 271:1990;325-329.
    • (1990) Biochem. J. , vol.271 , pp. 325-329
    • Tuchman, M.1    Holzknecht, R.A.2
  • 26
    • 0037444512 scopus 로고    scopus 로고
    • Fast-response proteomics by accelerated in-gel digestion of proteins
    • Havlis J., Thomas H., Sebela M., Shevchenko A. Fast-response proteomics by accelerated in-gel digestion of proteins. Anal. Chem. 75:2003;1300-1306.
    • (2003) Anal. Chem. , vol.75 , pp. 1300-1306
    • Havlis, J.1    Thomas, H.2    Sebela, M.3    Shevchenko, A.4
  • 27
    • 0023571665 scopus 로고
    • Import of rat ornithine transcarbamylase precursor into mitochondria: Two-step processing of the leader peptide
    • Sztul E.S., Hendrick J.P., Kraus J.P., Wall D., Kalousek F., Rosenberg L.E. Import of rat ornithine transcarbamylase precursor into mitochondria: two-step processing of the leader peptide. J. Cell Biol. 105:1987;2631-2639.
    • (1987) J. Cell Biol. , vol.105 , pp. 2631-2639
    • Sztul, E.S.1    Hendrick, J.P.2    Kraus, J.P.3    Wall, D.4    Kalousek, F.5    Rosenberg, L.E.6
  • 28
    • 0023663892 scopus 로고
    • Successive translocation into and out of the mitochondrial matrix: Targeting of proteins to the intermembrane space by a bipartite signal peptide
    • Hartl F.U., Ostermann J., Guiard B., Neupert W. Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptide. Cell. 51:1987;1027-1037.
    • (1987) Cell , vol.51 , pp. 1027-1037
    • Hartl, F.U.1    Ostermann, J.2    Guiard, B.3    Neupert, W.4
  • 29
    • 0024474942 scopus 로고
    • Biogenesis of cytochrome c1. Role of cytochrome c1 heme lyase and of the two proteolytic processing steps during import into mitochondria
    • Nicholson D.W., Stuart R.A., Neupert W. Biogenesis of cytochrome c1. Role of cytochrome c1 heme lyase and of the two proteolytic processing steps during import into mitochondria. J. Biol. Chem. 264:1989;10156-10168.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10156-10168
    • Nicholson, D.W.1    Stuart, R.A.2    Neupert, W.3
  • 30
    • 0018595957 scopus 로고
    • Inhibition by propionyl-coenzyme a of N -acetylglutamate synthetase in rat liver mitochondria. A possible explanation for hyperammonemia in propionic and methylmalonic acidemia
    • Coude F.X., Sweetman L., Nyhan W.L. Inhibition by propionyl-coenzyme A of. N -acetylglutamate synthetase in rat liver mitochondria. A possible explanation for hyperammonemia in propionic and methylmalonic acidemia J. Clin. Invest. 64:1979;1544-1551.
    • (1979) J. Clin. Invest. , vol.64 , pp. 1544-1551
    • Coude, F.X.1    Sweetman, L.2    Nyhan, W.L.3
  • 31
    • 0036894166 scopus 로고    scopus 로고
    • N -Acetylglutamate synthase deficiency and the treatment of hyperammonemic encephalopathy
    • Elpeleg O., Shaag A., Ben-Shalom E., Schmid T., Bachmann C. 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
  • 32
    • 0029052816 scopus 로고
    • The molecular basis of ornithine transcarbamylase deficiency: Modelling the human enzyme and the effects of mutations
    • Tuchman M., Morizono H., Reish O., Yuan X., Allewell N.M. The molecular basis of ornithine transcarbamylase deficiency: modelling the human enzyme and the effects of mutations. J. Med. Genet. 32:1995;680-688.
    • (1995) J. Med. Genet. , vol.32 , pp. 680-688
    • Tuchman, M.1    Morizono, H.2    Reish, O.3    Yuan, X.4    Allewell, N.M.5
  • 34
    • 0026537844 scopus 로고
    • Treatment of hyperammonemia with carbamylglutamate in rats
    • Grau E., Felipo V., Minana M.D., Grisolia S. Treatment of hyperammonemia with carbamylglutamate in rats. Hepatology. 15:1992;446-448.
    • (1992) Hepatology , vol.15 , pp. 446-448
    • Grau, E.1    Felipo, V.2    Minana, M.D.3    Grisolia, S.4
  • 38
    • 0025976652 scopus 로고
    • N -Acetylglutamate synthetase deficiency: Diagnosis, management and follow-up of a rare disorder of ammonia detoxification
    • Schubiger G., Bachmann C., Barben P., Colombo J.P., Tonz O., Schupbach D. N -Acetylglutamate synthetase deficiency: diagnosis, management and follow-up of a rare disorder of ammonia detoxification Eur. J. Pediatr. 150:1991;353-356.
    • (1991) Eur. J. Pediatr. , vol.150 , pp. 353-356
    • Schubiger, G.1    Bachmann, C.2    Barben, P.3    Colombo, J.P.4    Tonz, O.5    Schupbach, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.