메뉴 건너뛰기




Volumn 239, Issue 2, 1996, Pages 397-402

An essential lysine in the substrate-binding site of ornithine carbamoyltransferase

Author keywords

Affinity labeling; Carbamoyl phosphate binding site; Ornithine carbamoyltransferase

Indexed keywords

NORVALINE; ORNITHINE CARBAMOYLTRANSFERASE; PYRIDOXAL 5 PHOSPHATE;

EID: 0030055050     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0397u.x     Document Type: Article
Times cited : (10)

References (26)
  • 2
    • 0013927397 scopus 로고
    • La determinazione della ornitina carbamil transferasi serica nella diagnosi della epatite virale. Rapido micro ed ultra micro-metodo
    • Ceriotti, G. & Gazzaniga, A. (1966) La determinazione della ornitina carbamil transferasi serica nella diagnosi della epatite virale. Rapido micro ed ultra micro-metodo, Clin. Chim. Acta 14, 57-62.
    • (1966) Clin. Chim. Acta , vol.14 , pp. 57-62
    • Ceriotti, G.1    Gazzaniga, A.2
  • 3
    • 0027276542 scopus 로고
    • A comparative study on liver ornithine carbamoyltransferase from a marine mammal Stenella and an elasmobranch Sphyrna zygaena
    • De Gregorio, A., Valentini, G., Bellocco, E., Desideri, A. & Cuzzocrea, G. (1993) A comparative study on liver ornithine carbamoyltransferase from a marine mammal Stenella and an elasmobranch Sphyrna zygaena, Comp. Biochem. Physiol. B 105, 497-501.
    • (1993) Comp. Biochem. Physiol. B , vol.105 , pp. 497-501
    • De Gregorio, A.1    Valentini, G.2    Bellocco, E.3    Desideri, A.4    Cuzzocrea, G.5
  • 4
    • 0023031847 scopus 로고
    • Ligand-binding promoted conformational changes in yeast ornithine transcarbamoylase
    • Eisenstein, E. & Hensley, P. (1986) Ligand-binding promoted conformational changes in yeast ornithine transcarbamoylase, J. Biol. Chem. 261, 6192-6200.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6192-6200
    • Eisenstein, E.1    Hensley, P.2
  • 5
    • 0019879426 scopus 로고
    • Comparison of the essential arginine residue in Escherichia coli ornithine and aspartate transcarbamylases
    • Fortin, A. F., Hauber, J. M. & Kantrowitz, E. R. (1981) Comparison of the essential arginine residue in Escherichia coli ornithine and aspartate transcarbamylases, Biochim. Biophys. Acta 662, 8-14.
    • (1981) Biochim. Biophys. Acta , vol.662 , pp. 8-14
    • Fortin, A.F.1    Hauber, J.M.2    Kantrowitz, E.R.3
  • 6
    • 0026005119 scopus 로고
    • Control of L-ornithine specificity in Escherichia coli ornithine transcarbamoylase
    • Goldsmith, J. O., Lee, S., Zambidis, I. & Kuo, L. C. (1991) Control of L-ornithine specificity in Escherichia coli ornithine transcarbamoylase, J. Biol. Chem. 266, 18626-18634.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18626-18634
    • Goldsmith, J.O.1    Lee, S.2    Zambidis, I.3    Kuo, L.C.4
  • 7
    • 0021262303 scopus 로고
    • Structure and expression of a complementary DNA for the nuclear coded precursor of human mithocondrial ornithine transcarbamylase
    • Horwich, A. L., Fenton, W. A., Williams, K. R., Kalousec, F., Kraus, J. P., Doolittle, R. F., Konigsberg, W. & Rosenberg, L. E. (1984) Structure and expression of a complementary DNA for the nuclear coded precursor of human mithocondrial ornithine transcarbamylase, Science 224, 1068-1074.
    • (1984) Science , vol.224 , pp. 1068-1074
    • Horwich, A.L.1    Fenton, W.A.2    Williams, K.R.3    Kalousec, F.4    Kraus, J.P.5    Doolittle, R.F.6    Konigsberg, W.7    Rosenberg, L.E.8
  • 8
    • 0028352443 scopus 로고
    • Purification and properties of porcine liver ornithine transcarbamylase
    • Koger, J. B., Howell, R. G., Kelly, M. & Jones, E. E. (1994) Purification and properties of porcine liver ornithine transcarbamylase, Arch. Biochem. Biophys. 309, 293-299.
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 293-299
    • Koger, J.B.1    Howell, R.G.2    Kelly, M.3    Jones, E.E.4
  • 9
    • 0024261193 scopus 로고
    • Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: Role of arginine-57 in substrate binding and catalysis
    • Kuo, L. C., Miller, A. W., Lee, S. & Kozuma, C. (1988) Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: role of arginine-57 in substrate binding and catalysis, Biochemistry 27, 8823-8832.
    • (1988) Biochemistry , vol.27 , pp. 8823-8832
    • Kuo, L.C.1    Miller, A.W.2    Lee, S.3    Kozuma, C.4
  • 10
    • 0015343108 scopus 로고
    • The dual genetic control of ornithine carbamoyltransferase in Escherichia coli
    • Legrain, C., Halleux, P., Stalon, V. & Glansdorff, N. (1972) The dual genetic control of ornithine carbamoyltransferase in Escherichia coli, Eur. J. Biochem. 27, 93-102.
    • (1972) Eur. J. Biochem. , vol.27 , pp. 93-102
    • Legrain, C.1    Halleux, P.2    Stalon, V.3    Glansdorff, N.4
  • 11
    • 0017293245 scopus 로고
    • Ornithine carbamoyltransferase from Escherichia coli W
    • Legrain, C. & Stalon, V. (1976) Ornithine carbamoyltransferase from Escherichia coli W, Eur. J. Biochem. 63, 289-301.
    • (1976) Eur. J. Biochem. , vol.63 , pp. 289-301
    • Legrain, C.1    Stalon, V.2
  • 13
    • 0015522722 scopus 로고
    • Ornithine transcarbamylase from Streptococcus faecalis and bovine liver
    • Marshall, M. & Cohen, P. P. (1972) Ornithine transcarbamylase from Streptococcus faecalis and bovine liver, J. Biol. Chem. 247, 1654-1668.
    • (1972) J. Biol. Chem. , vol.247 , pp. 1654-1668
    • Marshall, M.1    Cohen, P.P.2
  • 14
    • 0017389805 scopus 로고
    • Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5′-phosphate
    • Marshall, M. & Cohen, P. P. (1977) Kinetics and equilibrium of the inactivation of ornithine transcarbamylases by pyridoxal 5′-phosphate, J. Biol. Chem. 252, 4276-4286.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4276-4286
    • Marshall, M.1    Cohen, P.P.2
  • 15
    • 0019321435 scopus 로고
    • Evidence for an exceptionally reactive arginyl residue at the binding site for carbamyl phosphate in bovine ornithine transcarbamylase
    • Marshall, M. & Cohen, P. P. (1980a) Evidence for an exceptionally reactive arginyl residue at the binding site for carbamyl phosphate in bovine ornithine transcarbamylase, J. Biol. Chem. 255, 7301-7305.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7301-7305
    • Marshall, M.1    Cohen, P.P.2
  • 16
    • 0019321417 scopus 로고
    • The essential sulphydryl group of ornithine transcarbamylases
    • Marshall, M. & Cohen, P. P. (1980b) The essential sulphydryl group of ornithine transcarbamylases, J. Biol. Chem. 255, 7296-7300.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7296-7300
    • Marshall, M.1    Cohen, P.P.2
  • 17
    • 0025179991 scopus 로고
    • Ligand-induced isomerizations of Escherichia coli ornithine transcarbamoylase
    • Miller, A. W. & Kuo, L. C. (1990) Ligand-induced isomerizations of Escherichia coli ornithine transcarbamoylase, J. Biol. Chem. 265, 15023-15027.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15023-15027
    • Miller, A.W.1    Kuo, L.C.2
  • 18
    • 0028921912 scopus 로고
    • Catabolic ornithine transcarbamylase of Halobacterium halobium (salinarium): Purification, characterization sequence determination, and evolution
    • Ruepp, A., Muller, H. N., Lottspeich, F. & Soppa, J. (1995) Catabolic ornithine transcarbamylase of Halobacterium halobium (salinarium): purification, characterization sequence determination, and evolution, J. Bacteriol. 177, 1129-1136.
    • (1995) J. Bacteriol. , vol.177 , pp. 1129-1136
    • Ruepp, A.1    Muller, H.N.2    Lottspeich, F.3    Soppa, J.4
  • 19
    • 0342416706 scopus 로고
    • Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of metallic complementation
    • Schachman, H. K., Panza, C. D., Navze, M., Karels, M. J., Wu, L. & Yang, Y. R. (1984) Location of amino acid alterations in mutants of aspartate transcarbamoylase: structural aspects of metallic complementation, Proc. Natl Acad. Sci. USA 81, 115-119.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 115-119
    • Schachman, H.K.1    Panza, C.D.2    Navze, M.3    Karels, M.J.4    Wu, L.5    Yang, Y.R.6
  • 20
    • 0027761310 scopus 로고
    • Fluorescence lifetimes of the tryptophan residues in ornithine transcarbamoylase
    • Shen, W. H. (1993) Fluorescence lifetimes of the tryptophan residues in ornithine transcarbamoylase, Biochemistiy 32, 13 925-13 932.
    • (1993) Biochemistiy , vol.32 , pp. 13925-13932
    • Shen, W.H.1
  • 21
    • 0028930481 scopus 로고
    • Mechanism-based enzyme inactivators
    • Silverman, R. B. (1995) Mechanism-based enzyme inactivators, Methods Enzymol. 249, 240-283.
    • (1995) Methods Enzymol. , vol.249 , pp. 240-283
    • Silverman, R.B.1
  • 22
    • 0020479450 scopus 로고
    • The primary structure of D-aminoacid oxidase from pig kidney, I-isolation and sequence of the tryptic peptides
    • Swenson, R. P., Williams, C. H. Jr, Massey, V., Ronchi, S., Minchiotti, L., Galliano, M. & Curti, B. (1982) The primary structure of D-aminoacid oxidase from pig kidney, I-isolation and sequence of the tryptic peptides, J. Biol. Chem. 257, 8817-8823.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8817-8823
    • Swenson, R.P.1    Williams Jr., C.H.2    Massey, V.3    Ronchi, S.4    Minchiotti, L.5    Galliano, M.6    Curti, B.7
  • 23
    • 0023791829 scopus 로고
    • Reactivity of the fructose 1,6-bisphosphate-activated pyruvate kinase from Escherichia coli with pyridoxal 5′-phosphate
    • Valentini, G., Speranza, M. L., Iadarola, P., Ferri, G. & Malcovati, M. (1988) Reactivity of the fructose 1,6-bisphosphate-activated pyruvate kinase from Escherichia coli with pyridoxal 5′-phosphate, Biol. Chem. Hoppe-Seyler 369, 1219-1226.
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 1219-1226
    • Valentini, G.1    Speranza, M.L.2    Iadarola, P.3    Ferri, G.4    Malcovati, M.5
  • 24
    • 0027381018 scopus 로고
    • Is pyridoxal 5′-phosphate an affinity label for phosphate-binding sites in proteins?: The case of glutamate dehydrogenase
    • Valinger, Z., Engel, P. C. & Metzler, D. E. (1993) Is pyridoxal 5′-phosphate an affinity label for phosphate-binding sites in proteins?: the case of glutamate dehydrogenase, Biochem. J. 294, 835-839.
    • (1993) Biochem. J. , vol.294 , pp. 835-839
    • Valinger, Z.1    Engel, P.C.2    Metzler, D.E.3
  • 25
    • 0017879465 scopus 로고
    • Anabolic ornithine carbamoyltransferase of Escherichia coli and catabolic ornithine carbamoyltransferase of Pseudomonas putida
    • Wargnies, B., Legrain, C. & Stalon, V. (1978) Anabolic ornithine carbamoyltransferase of Escherichia coli and catabolic ornithine carbamoyltransferase of Pseudomonas putida, Eur. J. Biochem. 89, 203-212.
    • (1978) Eur. J. Biochem. , vol.89 , pp. 203-212
    • Wargnies, B.1    Legrain, C.2    Stalon, V.3
  • 26
    • 0025359646 scopus 로고
    • Substrate specificity and protonation state of Escherichia coli ornithine transcarbamoylase as determined by pH studies
    • Zambidis, I. & Kuo, L. (1990) Substrate specificity and protonation state of Escherichia coli ornithine transcarbamoylase as determined by pH studies, J. Biol. Chem. 265, 2620-2623.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2620-2623
    • Zambidis, I.1    Kuo, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.