메뉴 건너뛰기




Volumn 113, Issue 4, 1996, Pages 809-816

Expression of horseshoe crab arginine kinase in Escherichia coli and site-directed mutations of the reactive cysteine peptide

Author keywords

arginine kinase; guanidino kinase; phosphagen

Indexed keywords

ARGININE KINASE;

EID: 0029888809     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/0305-0491(95)02104-3     Document Type: Article
Times cited : (25)

References (34)
  • 1
    • 0002640823 scopus 로고
    • Evolution of phosphagen kinases
    • Schoffeniels, E., ed. Amsterdam: North-Holland Publishing Co.
    • Watts, D.C. Evolution of phosphagen kinases. In: Schoffeniels, E., ed. Biochemical evolution and the origin of life. Amsterdam: North-Holland Publishing Co.; 1971: p. 151-173.
    • (1971) Biochemical Evolution and the Origin of Life , pp. 151-173
    • Watts, D.C.1
  • 2
    • 0001684572 scopus 로고
    • Evolution of phosphagen kinases in the chordate line
    • Watts, D.C. Evolution of phosphagen kinases in the chordate line. Symp. Zool. Soc. Lond. 36:105-127;1975.
    • (1975) Symp. Zool. Soc. Lond. , vol.36 , pp. 105-127
    • Watts, D.C.1
  • 3
    • 0002392633 scopus 로고
    • Guanidine compounds and phosphagens
    • Van Thoai, N.; Sheer, B.T., eds. New York: Gordon and Breach
    • Van Thoai, N.; Robin, R. Guanidine compounds and phosphagens. In: Van Thoai, N.; Sheer, B.T., eds. Chemical zoology, Vol. 14. New York: Gordon and Breach; 1969: p. 199-229.
    • (1969) Chemical Zoology , vol.14 , pp. 199-229
    • Van Thoai, N.1    Robin, R.2
  • 4
    • 0016077679 scopus 로고
    • Phosphagens and molecular evolution in worms
    • Robin, Y. Phosphagens and molecular evolution in worms. Biosystems 6:49-56;1974.
    • (1974) Biosystems , vol.6 , pp. 49-56
    • Robin, Y.1
  • 5
    • 0005114932 scopus 로고
    • Biological distribution of guanidines and phosphagens in marine annelida and related phyla from California, with a note on pluriphosphagens
    • Robin, Y. Biological distribution of guanidines and phosphagens in marine annelida and related phyla from California, with a note on pluriphosphagens. Comp. Biochem. Physiol. 12:347-367;1964.
    • (1964) Comp. Biochem. Physiol. , vol.12 , pp. 347-367
    • Robin, Y.1
  • 6
    • 0001797606 scopus 로고
    • Homologous phosphagen phosphokinases
    • Van Thoai, N.; Roche, J., eds. New York: Gordon and Breach
    • Van Thoai, N. Homologous phosphagen phosphokinases. In: Van Thoai, N.; Roche, J., eds. Homologous enzymes and biochemical evolution. New York: Gordon and Breach; 1968: p. 199-229.
    • (1968) Homologous Enzymes and Biochemical Evolution , pp. 199-229
    • Van Thoai, N.1
  • 7
    • 0002052737 scopus 로고
    • The origin and evolution of phosphagen phosphotransferases
    • Van Thoai, N.; Roche, J., eds. New York: Gordon and Breach
    • Watts, D.C. The origin and evolution of phosphagen phosphotransferases. In: Van Thoai, N.; Roche, J., eds. Homologous enzymes and biochemical evolution. New York: Gordon and Breach; 1968: p. 279-296.
    • (1968) Homologous Enzymes and Biochemical Evolution , pp. 279-296
    • Watts, D.C.1
  • 8
    • 0027486802 scopus 로고
    • Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle
    • Dumas, C; Camonis, J.H. Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle. J. Biol. Chem. 268: 21599-21605;1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21599-21605
    • Dumas, C.1    Camonis, J.H.2
  • 9
    • 0028212764 scopus 로고
    • Evolution of phosphagen kinase: Primary structure of glycocyamine kinase and arginine kinase from invertebrates
    • Suzuki, T.; Furukohri, T. Evolution of phosphagen kinase: primary structure of glycocyamine kinase and arginine kinase from invertebrates. J. Mol. Biol. 237:353-357;1994.
    • (1994) J. Mol. Biol. , vol.237 , pp. 353-357
    • Suzuki, T.1    Furukohri, T.2
  • 10
    • 0020654939 scopus 로고
    • Creatine kinase: Structure activity relationships
    • Kenyon, G.L.; Reed, G.H. Creatine kinase: structure activity relationships. Adv. Enzymol. 54:367-426;1983.
    • (1983) Adv. Enzymol. , vol.54 , pp. 367-426
    • Kenyon, G.L.1    Reed, G.H.2
  • 11
    • 0026793939 scopus 로고
    • The active site of creatine kinase affinity labeling of cysteine 282 with N-(2,3-epoxypropyl)-N-amidoglycine
    • Buechter, D.D.; Medzihradszky, K.; Burlingame, A.L.; Kenyon, G.L. The active site of creatine kinase affinity labeling of cysteine 282 with N-(2,3-epoxypropyl)-N-amidoglycine. J. Biol. Chem. 267:2173-2178;1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2173-2178
    • Buechter, D.D.1    Medzihradszky, K.2    Burlingame, A.L.3    Kenyon, G.L.4
  • 12
    • 0027268548 scopus 로고
    • Creatine kinase: The reactive cysteine is required for synergism but is nonessential for catalysis
    • Furter, R.; Furter-Graves, E.M.; Walliman, T. Creatine kinase: the reactive cysteine is required for synergism but is nonessential for catalysis. Biochemistry 32:7022-7029;1993.
    • (1993) Biochemistry , vol.32 , pp. 7022-7029
    • Furter, R.1    Furter-Graves, E.M.2    Walliman, T.3
  • 13
    • 0028236355 scopus 로고
    • Determination of the catalytic site of creatine kinase by site-directed mutagenesis
    • Lin, L; Perryman, M.B.; Friedman, D.; Roberts, R.; Ma T.S. Determination of the catalytic site of creatine kinase by site-directed mutagenesis. Biochim. Biophys. Acta 1206:97-104; 1994.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 97-104
    • Lin, L.1    Perryman, M.B.2    Friedman, D.3    Roberts, R.4    Ma, T.S.5
  • 15
    • 0024355968 scopus 로고
    • Phosphocreatine represents a thermodynamic and functional improvement over other muscle phosphagens
    • Ellington, W.R. Phosphocreatine represents a thermodynamic and functional improvement over other muscle phosphagens. J. Exp. Biol. 143:177-194;1989.
    • (1989) J. Exp. Biol. , vol.143 , pp. 177-194
    • Ellington, W.R.1
  • 16
    • 0027133018 scopus 로고
    • Horseshoe crab sperm contain a unique isoform of arginine kinase which is present in midpiece and flagellum
    • Strong, S.J.; Ellington, W.R. Horseshoe crab sperm contain a unique isoform of arginine kinase which is present in midpiece and flagellum. J. Exp. Zool. 267:563-571;1993.
    • (1993) J. Exp. Zool. , vol.267 , pp. 563-571
    • Strong, S.J.1    Ellington, W.R.2
  • 17
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequence of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C.; Viera, J.; Messing, J. Improved M13 phage cloning vectors and host strains: nucleotide sequence of the M13mp18 and pUC19 vectors. Gene 33:103-119;1985.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Viera, J.2    Messing, J.3
  • 20
    • 0028858939 scopus 로고
    • Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: Insights into catalytically important residues
    • Strong, S.J.; Ellington, W.R. Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues. Biochim. Biophys. Acta 1246:197-200;1995.
    • (1995) Biochim. Biophys. Acta , vol.1246 , pp. 197-200
    • Strong, S.J.1    Ellington, W.R.2
  • 21
    • 0002100787 scopus 로고
    • A rapid screening procedure for the identification of bacterial recombinant clones
    • Sekar, V. A rapid screening procedure for the identification of bacterial recombinant clones. Biotechnology 5:11-13;1987.
    • (1987) Biotechnology , vol.5 , pp. 11-13
    • Sekar, V.1
  • 23
    • 0024323295 scopus 로고
    • A general methods of site-specific mutagenesis using a modification of PCR
    • Nelson, R.M.; Long, G.L. A general methods of site-specific mutagenesis using a modification of PCR. Anal. Biochem. 180: 147-151;1989.
    • (1989) Anal. Biochem. , vol.180 , pp. 147-151
    • Nelson, R.M.1    Long, G.L.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during assembly of the head bacteriophage T4. Nature Lond. 227:680-685;1970.
    • (1970) Nature Lond. , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254;1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 27
    • 0025064677 scopus 로고
    • Mitochondrial arginine kinase from the heart of the horseshoe crab, Limulus polyphemus, 2. Catalytic properties and studies of potential functional coupling with oxidative phosphorylation
    • Doumen, C.; Ellington, W.R. Mitochondrial arginine kinase from the heart of the horseshoe crab, Limulus polyphemus, 2. Catalytic properties and studies of potential functional coupling with oxidative phosphorylation. J. Comp. Physiol. B 160:459-468;1990.
    • (1990) J. Comp. Physiol. B , vol.160 , pp. 459-468
    • Doumen, C.1    Ellington, W.R.2
  • 28
  • 29
    • 11944270350 scopus 로고
    • Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzyme
    • Babbit, P.C.; West, B.L.; Beuchter, D.D.; Kuntz, I.D.; Kemyon, G.L. Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzyme. Biotechnology 8:945-949;1990.
    • (1990) Biotechnology , vol.8 , pp. 945-949
    • Babbit, P.C.1    West, B.L.2    Beuchter, D.D.3    Kuntz, I.D.4    Kemyon, G.L.5
  • 30
    • 0025947345 scopus 로고
    • Cloning and expression of functional rabbit muscle creatine kinase in Escherichia coli
    • Chen, L.H.; Babbit, P.C.; Vasquez, J.R.; West, B.L.; Kenyon, G.L. Cloning and expression of functional rabbit muscle creatine kinase in Escherichia coli. J. Biol. Chem. 266:12053-12057;1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12053-12057
    • Chen, L.H.1    Babbit, P.C.2    Vasquez, J.R.3    West, B.L.4    Kenyon, G.L.5
  • 33
    • 0016794481 scopus 로고
    • Comparative structural studies of the active site of guanidino phosphotransferases
    • Brevet, A.; Zeitoun, Y.; Pradel, L.A. Comparative structural studies of the active site of guanidino phosphotransferases. Biochim. Biophys. Acta 393:1-9;1975.
    • (1975) Biochim. Biophys. Acta , vol.393 , pp. 1-9
    • Brevet, A.1    Zeitoun, Y.2    Pradel, L.A.3
  • 34
    • 0015241458 scopus 로고
    • The essential cysteine peptide of lombricine kinase from Lumbricus terrestris muscle
    • der Terrosian, E.; Desvages, C.; Pradel, L.A.; Kassab, R.; van Thoai, N. The essential cysteine peptide of lombricine kinase from Lumbricus terrestris muscle. Eur. J. Biochem. 22:585-592; 1971.
    • (1971) Eur. J. Biochem. , vol.22 , pp. 585-592
    • Der Terrosian, E.1    Desvages, C.2    Pradel, L.A.3    Kassab, R.4    Van Thoai, N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.