Evidence that amino-acid residues are responsible for substrate synergism of locust arginine kinase

Insect Biochemistry and Molecular Biology

Volumn 38, Issue 1, 2008, Pages 59-65

  Wu, Qing Yun ^a   Li, Feng ^a   Wang, Xiao Yun ^a  

^a SHANDONG AGRICULTURAL UNIVERSITY   (China)

Author keywords

Arginine kinase; Conformational change; Kinetic parameter; Locust; Mutagenesis; Synergism

Indexed keywords

AMINO ACID; ARGININE KINASE;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BINDING SITE; ENZYMOLOGY; GENE EXPRESSION; GENETICS; KINETICS; LOCUST; METABOLISM; MOLECULAR GENETICS; SITE DIRECTED MUTAGENESIS; SPECTROFLUOROMETRY;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; ARGININE KINASE; BINDING SITES; GENE EXPRESSION; KINETICS; LOCUSTA MIGRATORIA; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; SPECTROMETRY, FLUORESCENCE;

LOCUSTA MIGRATORIA MANILENSIS;

EID: 36749058847     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2007.09.004     Document Type: Article

References (25)

1. Bradford M.M. A rapid and sensitive method for the quantination of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
2. Cleland W.W. Statistical analysis of enzyme kinetic data. Methods Enzymol 63 (1979) 103-138
3. Compaan D.M., and Ellington W.R. Functional consequences of a gene duplication and fusion event in an arginine kinase. J. Exp. Biol. 206 (2003) 1545-1556
4. Ellington W.R. Evolution and physiological roles of phosphagen systems. Annu. Rev. Physiol. 63 (2001) 289-325
5. France R.M., Cellers D.S., and Grossman S.H. Purification, characterization, and hydrodynamic properties of arginine kinase from Gulf Shrimp (Penaeus aztecus). Arch. Biochem. Biophys. 345 (1997) 73-78
6. Fujimoto N., Tanaka K., and Suzuki T. Amino acid residues 62 and 193 play the key role in regulating the synergism of substrate binding in oyster arginine kinase. FEBS Lett 579 (2005) 1688-1692
7. Gao X.X., and Harris T.K. Steady-state kinetic mechanism of PDK1. J. Biol. Chem. 281 (2006) 21670-21681
8. Grossman S.H. Interaction of creatine kinase from monkey brain with substrate: analysis of kinetics and fluorescence polarization. J. Neurochem. 41 (1983) 729-736
9. Guo Q., Zhao F., and Guo S.Y. The tryptophane residues of dimeric arginine kinase: roles of Trp-208 and Trp-218 in active site and conformation stability. Biochimie 86 (2004) 379-386
10. Hornemann T., Rutishauser D., and Wallimann T. Why is creatine kinase a dimer? Evidence for cooperativity between the two subunits. Biochim. Biophys. Acta 1480 (2000) 365-373
11. - creatine transition-state analogue complex. Biochemistry 41 (2002) 13861-13867
12. Li M., Wang X.Y., and Bai J.G.. Purification and characterization of arginine kinase from Locust. Protein Pept. Lett. 13 (2006) 405-410
13. 3-blocked creatine kinase with altered catalytic activity. Kinetic consequences of the presence of the blocking group. J. Biol. Chem. 252 (1977) 1202-1207
14. Morrison J.F., and James E. The mechanism of the reaction catalyzed by adenosine triphosphate-creatine phosphotransferase. Biochem. J. 97 (1965) 37-52
15. Muhlebach S.M., Gross M., Wirz T., Wallimann T., Perriard J.C., and Wyss M. Sequence homology and structure predictions of the creatine kinase isoenzymes. Mol. Cell. Biochem. 133 (1994) 245-262
16. Novak W.R., Wang P.F., McLeish M.J., Kenyon G.L., and Babbitt P.C. Isoleucine 69 and valine 325 form a specificity pocket in human muscle creatine kinase. Biochemistry 43 (2004) 13766-13774
17. Pereira C.A., Alonso G.D., and Paveto M.C. Trypanosoma cruzi arginine kinase characterization and cloning. J. Biol. Chem. 275 (2000) 1495-1501
18. Schlattner U., Eder M., Dolder M., Khuchua Z.A., Strauss A.W., and Wallimann T. Divergent enzyme kinetics and structural properties of the two human mitochondrial creatine kinase isoenzymes. Biol. Chem. 381 (2000) 1063-1070
19. Suzuki T., and Furukohri T. Evolution of phosphagen kinase. Primary structure of glycocyamine kinase and arginine kinase from invertebrates. J. Mol. Biol. 237 (1994) 353-357
20. Tanaka K., Ichinaria S., Iwanamia K., Yoshimatsub S., and Suzuki T. Arginine kinase from the beetle Cissites cephalotes (Olivier). Molecular cloning, phylogenetic analysis and enzymatic properties. Insect Biochem. Mol. Biol. 37 (2007) 338-345
21. Uda K., and Suzuki T. Role of amino acid residues on the GS region of Stichopus arginine kinase and Danio creatine kinase. Protein J 23 (2004) 53-64
22. Wu, Q.Y., Li, F., Zhu, W.J., Wang, X.Y., 2007. Cloning, expression, purification, and characterization of arginine kinase from Locusta migratoria manilensis. Comp. Biochem. Physiol. B, doi:10.1016/j.cbpb.2007.07.002.
23. Wyss M., Smeitink J., and Wevers R.A. Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism. Biochim. Biophys. Acta 1102 (1992) 119-166
24. Yousef M.S., Clark S.A., Pruett P.K., Somasundaram T., Ellington W.R., and Chapman M.S. Induced fit in guanidino kinases-comparison of substrate-free and transition state analog structures of arginine kinase. Protein Sci 12 (2003) 103-111
25. Zhou G., Somasundaram T., Blanc E., Parthasarathy G., Ellington W.R., and Chapman M.S. Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions. Proc. Natl. Acad. Sci. 15 (1998) 8449-8454