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Volumn 61, Issue 1, 2004, Pages 110-117

Unique evolution of Bivalvia arginine kinases

Author keywords

Arginine kinase; Crassostrea; Kinetic property; Scapharca; Two domain enzyme

Indexed keywords

AMINO ACID; ARGININE; ARGININE KINASE; ASPARTIC ACID; GLYCINE; LYSINE;

EID: 1642458394     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-3384-1     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 0002052737 scopus 로고
    • The origin and evolution of phosphagen phosphotransferases
    • Van Thoai N. and Roche J. (eds), Gordon and Breach, New York
    • Watts D. C. (1968) The origin and evolution of phosphagen phosphotransferases. In: Homologous Enzymes and Biochemical Evolution, pp. 279-296, Van Thoai N. and Roche J. (eds), Gordon and Breach, New York
    • (1968) Homologous Enzymes and Biochemical Evolution , pp. 279-296
    • Watts, D.C.1
  • 2
    • 0001797606 scopus 로고
    • Homologous phosphagen phosphokinases
    • Van Thoai N. and Roche J. (eds), Gordon and Breach, New York
    • Van Thoai N. (1968) Homologous phosphagen phosphokinases. In: Homologous Enzymes and Biochemical Evolution, pp. 199-229, Van Thoai N. and Roche J. (eds), Gordon and Breach, New York
    • (1968) Homologous Enzymes and Biochemical Evolution , pp. 199-229
    • Van Thoai, N.1
  • 3
    • 77956932220 scopus 로고
    • Arginine kinase and other invertebrate guanidino kinases
    • Boyer P. C. (ed.), Academic Press, New York
    • Morrison J. F. (1973) Arginine kinase and other invertebrate guanidino kinases. In: The Enzymes, pp. 457-486, Boyer P. C. (ed.), Academic Press, New York
    • (1973) The Enzymes , pp. 457-486
    • Morrison, J.F.1
  • 4
    • 0020654939 scopus 로고
    • Creatine kinase: Structure-activity relationships
    • Kenyon G. L. and Reed G. H. (1986) Creatine kinase: structure-activity relationships. Adv. Enzymol. 54: 367-426
    • (1986) Adv. Enzymol. , vol.54 , pp. 367-426
    • Kenyon, G.L.1    Reed, G.H.2
  • 6
    • 0028212764 scopus 로고
    • Evolution of phosphagen kinase: Primary structure of glycocyamine kinase and arginine kinase from invertebrates
    • Suzuki T. and Furukohri T. (1994) Evolution of phosphagen kinase: primary structure of glycocyamine kinase and arginine kinase from invertebrates. J. Mol. Biol. 237: 353-357
    • (1994) J. Mol. Biol. , vol.237 , pp. 353-357
    • Suzuki, T.1    Furukohri, T.2
  • 7
    • 0031555335 scopus 로고    scopus 로고
    • Evolution of phosphagen kinase. VI. Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site
    • Suzuki T., Kawasaki Y., Furukohri T. and Ellington W. R. (1997) Evolution of phosphagen kinase. VI. Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site. Biochim. Biophys. Acta 1343: 152-159
    • (1997) Biochim. Biophys. Acta , vol.1343 , pp. 152-159
    • Suzuki, T.1    Kawasaki, Y.2    Furukohri, T.3    Ellington, W.R.4
  • 8
    • 0033564680 scopus 로고    scopus 로고
    • Arginine kinase evolved twice: Evidence that echinoderm arginine kinase originated from creatine kinase
    • Suzuki T., Kamidochi M., Inoue N., Kawamichi H., Yazawa Y., Furukohri T. et al. (1999) Arginine kinase evolved twice: evidence that echinoderm arginine kinase originated from creatine kinase. Biochem. J. 340: 671-675
    • (1999) Biochem. J. , vol.340 , pp. 671-675
    • Suzuki, T.1    Kamidochi, M.2    Inoue, N.3    Kawamichi, H.4    Yazawa, Y.5    Furukohri, T.6
  • 9
    • 0002640823 scopus 로고
    • Evolution of phosphagen kinases
    • Schoffeniels E. (ed.), North-Holland, Amsterdam
    • Watts D. C. (1971) Evolution of phosphagen kinases. In: Biochemical Evolution and the Origin of Life, pp. 150-173, Schoffeniels E. (ed.), North-Holland, Amsterdam
    • (1971) Biochemical Evolution and the Origin of Life , pp. 150-173
    • Watts, D.C.1
  • 10
    • 0001684572 scopus 로고
    • Evolution of phosphagens along the chordate line
    • Watts D. C. (1975) Evolution of phosphagens along the chordate line. Symp. Zool. Soc. Lond. 36: 105-127
    • (1975) Symp. Zool. Soc. Lond. , vol.36 , pp. 105-127
    • Watts, D.C.1
  • 11
    • 0030671447 scopus 로고    scopus 로고
    • Evolution of phosphagen kinase: Isolation, characterization and cDNA-derived amino acid sequence of two-domain arginine kinase from the sea anemone Anthopleura japonicus
    • Suzuki T., Kawasaki Y. and Furukohri T. (1997) Evolution of phosphagen kinase: isolation, characterization and cDNA-derived amino acid sequence of two-domain arginine kinase from the sea anemone Anthopleura japonicus. Biochem. J. 328: 301-306
    • (1997) Biochem. J. , vol.328 , pp. 301-306
    • Suzuki, T.1    Kawasaki, Y.2    Furukohri, T.3
  • 12
    • 0026698727 scopus 로고
    • Mitochondrial creatine kinase: A key enzyme of aerobic energy metabolism
    • Wyss M., Smeitink J., Wevers R. A. and Wallimann T. (1992) Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism. Biochim. Biophys. Acta 1102: 119-166
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 119-166
    • Wyss, M.1    Smeitink, J.2    Wevers, R.A.3    Wallimann, T.4
  • 13
    • 0002508208 scopus 로고    scopus 로고
    • Purification and characterization of arginine kinase from mactrin adductor muscle
    • Soga T. and Yazawa Y. (1996) Purification and characterization of arginine kinase from mactrin adductor muscle (abstract). Zool. Sci. 13 (suppl.): 55
    • (1996) Zool. Sci. , vol.13 , Issue.SUPPL. , pp. 55
    • Soga, T.1    Yazawa, Y.2
  • 14
    • 0032517306 scopus 로고    scopus 로고
    • Gene duplication and fusion have occurred frequently in the evolution of phosphagen kinases - A two-domain arginine kinase from the clam Pseudocardium sachalinensis
    • Suzuki T., Kawasaki Y., Unemi Y., Nishimura Y., Soga T., Kamidochi K. et al. (1998) Gene duplication and fusion have occurred frequently in the evolution of phosphagen kinases - a two-domain arginine kinase from the clam Pseudocardium sachalinensis. Biochim. Biophys. Acta 1388: 253-259
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 253-259
    • Suzuki, T.1    Kawasaki, Y.2    Unemi, Y.3    Nishimura, Y.4    Soga, T.5    Kamidochi, K.6
  • 15
    • 0035986619 scopus 로고    scopus 로고
    • Two-domain arginine kinases from the clams Solen strictus and Corbicula japonica: Exceptional amino acid replacement of the functionally important D62 by G
    • Suzuki T., Sugimura N., Taniguchi T., Unemi Y., Murata T., Hayashida M. et al. (2002) Two-domain arginine kinases from the clams Solen strictus and Corbicula japonica: exceptional amino acid replacement of the functionally important D62 by G. Int. J. Biochem. Cell Biol. 34: 1221-1229
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 1221-1229
    • Suzuki, T.1    Sugimura, N.2    Taniguchi, T.3    Unemi, Y.4    Murata, T.5    Hayashida, M.6
  • 16
    • 0038369013 scopus 로고    scopus 로고
    • Functional consequences of a gene duplication and fusion event in an arginine kinase
    • Compaan D. M. and Ellington W. R. (2003) Functional consequences of a gene duplication and fusion event in an arginine kinase. J. Exp. Biol. 206: 1545-1556
    • (2003) J. Exp. Biol. , vol.206 , pp. 1545-1556
    • Compaan, D.M.1    Ellington, W.R.2
  • 17
    • 0034604566 scopus 로고    scopus 로고
    • Arginine kinase from Nautilus pompilius, a living fossil: Site-directed mutagenesis studies on the role of amino acid residues in GS (guanidino specificity) region
    • Suzuki T., Fukuta H., Nagato H. and Umekawa M. (2000) Arginine kinase from Nautilus pompilius, a living fossil: site-directed mutagenesis studies on the role of amino acid residues in GS (guanidino specificity) region. J. Biol. Chem. 275: 23884-23890
    • (2000) J. Biol. Chem. , vol.275 , pp. 23884-23890
    • Suzuki, T.1    Fukuta, H.2    Nagato, H.3    Umekawa, M.4
  • 18
    • 0034331815 scopus 로고    scopus 로고
    • Stichopus japonicus arginine kinase: Gene structure and unique substrate recognition system
    • Suzuki T., Yamamoto Y. and Umekawa M. (2000) Stichopus japonicus arginine kinase: gene structure and unique substrate recognition system. Biochem. J. 351: 579-585
    • (2000) Biochem. J. , vol.351 , pp. 579-585
    • Suzuki, T.1    Yamamoto, Y.2    Umekawa, M.3
  • 19
    • 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. and Ellington W. R. (1995) 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) Biochim. Biophys. Acta , vol.1246 , pp. 197-200
    • Strong, S.J.1    Ellington, W.R.2
  • 20
    • 0024355968 scopus 로고
    • Phosphocreatine represents a thermodynamic and functional improvement over other muscle phosphagens
    • Ellington W. R. (1989) Phosphocreatine represents a thermodynamic and functional improvement over other muscle phosphagens. J. Exp. Biol. 143: 177-194
    • (1989) J. Exp. Biol. , vol.143 , pp. 177-194
    • Ellington, W.R.1
  • 21
    • 0017757299 scopus 로고
    • Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle
    • Wallimann T., Turner D. C. and Eppenberger H. M. (1977) Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle. J. Cell. Biol. 75: 297-317
    • (1977) J. Cell. Biol. , vol.75 , pp. 297-317
    • Wallimann, T.1    Turner, D.C.2    Eppenberger, H.M.3
  • 22
    • 0001838147 scopus 로고
    • The mechanism of the reaction catalyzed by adenosine triphosphate- creatine phosphotransferase
    • Morrison J. F. and James E. (1965) The mechanism of the reaction catalyzed by adenosine triphosphate-creatine phosphotransferase. Biochem. J. 97: 37-52
    • (1965) Biochem. J. , vol.97 , pp. 37-52
    • Morrison, J.F.1    James, E.2
  • 23
    • 0037413850 scopus 로고    scopus 로고
    • Kinetic properties and structural characteristics of an unusual two-domain arginine kinase of the clam Corbicula japonica
    • Suzuki T., Tomoyuki T. and Uda K. (2003) Kinetic properties and structural characteristics of an unusual two-domain arginine kinase of the clam Corbicula japonica. FEBS Lett. 533: 95-98
    • (2003) FEBS Lett. , vol.533 , pp. 95-98
    • Suzuki, T.1    Tomoyuki, T.2    Uda, K.3
  • 24
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W. (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol. 63: 103-138
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 28
    • 0003437299 scopus 로고
    • Distributed by the author. Department of Genetics, University of Washington, Seattle, USA
    • Felsenstein J. (1993) PHYLIP (Phylogeny Inference Package) version 3.5c. Distributed by the author. Department of Genetics, University of Washington, Seattle, USA
    • (1993) PHYLIP (Phylogeny Inference Package) Version 3.5c
    • Felsenstein, J.1
  • 29
    • 0029836454 scopus 로고    scopus 로고
    • Quartet puzzling: A quartet maximum likelihood method for reconstructing tree topologies
    • Strimmer K., and Haeseler A. von (1996) Quartet puzzling: a quartet maximum likelihood method for reconstructing tree topologies. Mol. Biol. Evol. 13: 964-969
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 964-969
    • Strimmer, K.1    Von Haeseler, A.2
  • 30
    • 0021981156 scopus 로고
    • Studies on phosphagen synthesis by mitochondrial preparations
    • Hird F. J. and Robin Y. (1985) Studies on phosphagen synthesis by mitochondrial preparations. Comp. Biochem. Physiol. 80B: 517-520
    • (1985) Comp. Biochem. Physiol. , vol.80 B , pp. 517-520
    • Hird, F.J.1    Robin, Y.2
  • 31
    • 0023955778 scopus 로고
    • Cytoplasmic and mitochondrial arginine kinases in Drosophila: Evidence for a single gene
    • Munneke L. R. and Collier G. E. (1988) Cytoplasmic and mitochondrial arginine kinases in Drosophila: evidence for a single gene. Biochem. Genet. 26: 131-141
    • (1988) Biochem. Genet. , vol.26 , pp. 131-141
    • Munneke, L.R.1    Collier, G.E.2
  • 32
    • 0025173197 scopus 로고
    • Mitochondrial arginine kinase from the heart of the horseshoe crab, Limulus polyphemus. I. Physico-chemical properties and nature of interaction with the mitochondrion
    • Doumen C. and Ellington W. R. (1990) Mitochondrial arginine kinase from the heart of the horseshoe crab, Limulus polyphemus. I. Physico-chemical properties and nature of interaction with the mitochondrion. J. Comp. Physiol. 160: 449-457
    • (1990) J. Comp. Physiol. , vol.160 , pp. 449-457
    • Doumen, C.1    Ellington, W.R.2
  • 33
    • 0030671248 scopus 로고    scopus 로고
    • Mitochondrial arginine kinase in the midgut of the tobacco hornworm (Manduca sexta)
    • Chamberlin M. (1997) Mitochondrial arginine kinase in the midgut of the tobacco hornworm (Manduca sexta) J. Exp. Biol. 200: 2789-2796
    • (1997) J. Exp. Biol. , vol.200 , pp. 2789-2796
    • Chamberlin, M.1
  • 34
    • 0000157596 scopus 로고
    • Mitochondrial activities of phosphagen kinases are not widely distributed in the invertebrates
    • Ellington W. R. and Hines A. C. (1991) Mitochondrial activities of phosphagen kinases are not widely distributed in the invertebrates. Biol. Bull. 180: 505-507
    • (1991) Biol. Bull. , vol.180 , pp. 505-507
    • Ellington, W.R.1    Hines, A.C.2


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