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== Structural Highlights ==
== Structural Highlights ==
The structure of arginine kinase is mainly α-helical and contains an N-terminal region <ref>PMID:9671698</ref>. However, when compared to creatine kinase, arginine kinase is not terminated with a pair of proline-glycine. Proline typically restricts change in conformation and is the amino acid that terminates helices, while glycine is associated with flexibility.  On the C-terminal end, there are eight-stranded antiparallel β-sheets with seven α-helices flanking them <ref>PMID:9671698</ref>.  
The structure of arginine kinase is mainly α-helical and contains an N-terminal region <ref>PMID:9671698</ref>. However, when compared to creatine kinase, arginine kinase is not terminated with a pair of proline-glycine. Proline typically restricts change in conformation and is the amino acid that terminates helices, while glycine is associated with flexibility.  On the C-terminal end, there are eight-stranded antiparallel β-sheets with seven α-helices flanking them <ref>PMID:9671698</ref>.  
The small domain specificity loop forms a “specificity” pocket surrounding the methyl substituent of the guanidinium group that is unique to creatine substrates.  In this region, five residues differ between arginine and creatine kinases: 312, 314, 315, 317, and 319 <ref>Newsholme, E. A., Beis, I., Leech, A. R., & Zammit, V. A. (1978). The role of creatine
The small domain specificity loop forms a “specificity” pocket surrounding the methyl substituent of the guanidinium group that is unique to creatine substrates.  In this region, five residues differ between arginine and creatine kinases: 312, 314, 315, 317, and 319 <ref>Newsholme, E. A., Beis, I., Leech, A. R., & Zammit, V. A. (1978). The role of creatine
kinase and arginine kinase in muscle. Biochemical Journal, 172(3), 533–537</ref>. Within each arginine kinase, there is typically a Mg+2 ion adjacent to the antiparallel β-sheet <ref>PMID:9671698</ref>. Typically two arginine kinase structures mirror each other and form a hole like structure in between the two.  However, when a substrate is in the binding site, the active site remains unchanged and does not change in conformation <ref>PMID:9671698</ref>.  
kinase and arginine kinase in muscle. Biochemical Journal, 172(3), 533–537</ref>. Within each arginine kinase, there is typically a Mg+2 ion adjacent to the antiparallel β-sheet <ref>PMID:9671698</ref>. Typically two arginine kinase structures mirror each other and form a hole like structure in between the two.  However, when a substrate is in the binding site, the active site remains unchanged and does not change in conformation <ref>PMID:9671698</ref>.  
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& Flawia, M. M. (2000) Trypanosoma cruzi arginine kinase characterization and
& Flawia, M. M. (2000) Trypanosoma cruzi arginine kinase characterization and
cloning., J. Biol.Chem. 275, 1495-1501.</ref>.  
cloning., J. Biol.Chem. 275, 1495-1501.</ref>.  
Arginine Kinase is a phosphokinase - a kinase used in the catalyzation of phosphagens and adenosine diphosphate (ADP) into adenosine triphosphate (ATP). Phosphagens act as a storage form of phosphate (Nω-phospho-L-arginine) that can be catalyzed into an energy source (ATP) when needed <ref>http://www.jbc.org/content/275/2/1495.full.pdf</ref>. The arginine kinase is a lock and key catalyst that holds ADP and phosphoarginine in place and catalyzes the transfer of inorganic phosphate on phosphoarginine to ADP and forms of arginine and ATP <ref>DOI 10.1110/ps.03428304</ref>.
Arginine Kinase is a phosphokinase - a kinase used in the catalyzation of phosphagens and adenosine diphosphate (ADP) into adenosine triphosphate (ATP). Phosphagens act as a storage form of phosphate (Nω-phospho-L-arginine) that can be catalyzed into an energy source (ATP) when needed <ref>http://www.jbc.org/content/275/2/1495.full.pdf</ref>. The arginine kinase is a lock and key catalyst that holds ADP and phosphoarginine in place and catalyzes the transfer of inorganic phosphate on phosphoarginine to ADP and forms of arginine and ATP <ref>DOI 10.1110/ps.03428304</ref>.
== Application to the Animal Kingdom ==  
== Application to the Animal Kingdom ==  
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Drosophila Melanogaster." Www.onlinelibrary.wiley.com. Laboratory of
Drosophila Melanogaster." Www.onlinelibrary.wiley.com. Laboratory of
Developmental Biology, Swiss Federal Institute of Technology, Zurich, 21 June 1973. Web. 12 Nov. 2015</ref>
Developmental Biology, Swiss Federal Institute of Technology, Zurich, 21 June 1973. Web. 12 Nov. 2015</ref>
Arginine Kinase (AK) is represented by a single gene and the sequence or partial sequence is available from Drosophila, Limulus, lobster, shrimp, and abalone <ref>Wang, Yu-mei E., Pia Esbensen, and David Bentley. "Arginine Kinase Expression and
Arginine Kinase (AK) is represented by a single gene and the sequence or partial sequence is available from Drosophila, Limulus, lobster, shrimp, and abalone <ref>Wang, Yu-mei E., Pia Esbensen, and David Bentley. "Arginine Kinase Expression and
Localization in Growth Cone Migration." The Journal of Neuroscience 18.3
Localization in Growth Cone Migration." The Journal of Neuroscience 18.3