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<Structure load='3M10' size='350' frame='true' align='right' caption='The 3D structure of a bound confirmation of Arginine Kinase' scene='Insert optional scene name here' />
==Arginine Kinase==
==Arginine Kinase==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
A phosphokinase used to store energy in the form of Argininephosphate.  
This is a default text for your page '''Michael Adams/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
== Isolation ==
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
In Strong and Ellington’s 1994 experiment, arginine kinase (AK) was isolated from <i>Limulus polyphemus</i>, the Atlantic horseshoe crab, a marine chelicerate arthropod. They isolated the gene for AK, sequenced the DNA and identified it to be 1071 nucleotides. The 1071 nucleotides produce a 357 amino acid protein and AK extracted from other organisms show similarity to this protein. AK serves a similar function to that of creatine kinase, in vertebrates <ref>Strong, S., & Ellington, W. (1994). Isolation and sequence analysis of the gene for
== Isolation Methods ==
arginine kinase from the chelicerate arthropod, Limulus polyphemus: Insights into
In Strong and Ellington’s 1994 experiment, arginine kinase (AK) was isolated from Limulus polyphemus, the Atlantic horseshoe crab, a marine chelicerate arthropod. They isolated the gene for AK and sequenced the DNA and produced a full genome breakdown of the 1071 nucleotide gene. The 1071 nucleotides translate to a 357 amino acid protein that is extensively similar to AK’s extracted from other organisms. It also provides a similar function to that of creatine kinase, in vertebrates (Strong and Ellington, 1994).  
catalytically important residues. Biochimica Et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 197-200.</ref>. The enzyme creatine kinase maintains energy homeostasis by producing ATP in high energy requiring cells such as skeletal and cardiac muscle and neurons <ref name=wallimann1973>Wallimann, Theo, and Hans M. Eppenberger. "Properties of Arginine Kinase from
== Structural highlights ==
Drosophila Melanogaster." Www.onlinelibrary.wiley.com. Laboratory of
The structure of arginine kinase is mainly α-helical and contains an N-terminal region (Figure 1b). 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 (Figure 1).  
Developmental Biology, Swiss Federal Institute of Technology, Zurich, 21 June 1973. Web. 12 Nov. 2015</ref>. This is done by the transfer of an N-phosphoryl group from phosphocreatine to ADP.  
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 (Newsholme et al, 1978). Within each arginine kinase, there is typically a Mg+2 ion adjacent to the antiparallel β-sheet (Figure 1b). 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 (Figure 1a).
== Structure ==
== Function ==
The structure of <scene name='71/716599/My3/1'>arginine kinase</scene> is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding.  (Figure 2). However, when compared to creatine kinase, arginine kinase is not terminated at the N-terminal end with a pair of proline-glycine residues. Typically within creatine kinase, the proline molecules restrict changes in conformation and is the amino acid that terminates helices. The glycine chains are usually associated with flexibility. However, in arginine kinase this is typically not the case. On the C-terminal end, there is an eight-stranded antiparallel <scene name='71/716599/Beta/1'>β-sheet</scene> with seven <scene name='71/716599/Mynewscene/1'>α-helices</scene> flanking the sheet (Figure 1). Residue <scene name='71/716599/330/2'>330</scene> is an arginine that appears to play a crucial role in maintaining structural stability. Studies show that a mutation in the residue leads to a steep decline in enzymatic activity <ref>DOI 10.1016/j.ijbiomac.2012.12.015</ref>.  
Arginine Kinase is part of a class of kinases that regulates ATP levels in the body to help maintain homeostasis.  It creates a sort of storage option for ATP.  It is the most common phosphokinase (PK) in invertebrates. The most common PK in vertebrates is Creatine Kinase (Pereira et al, 2000).  
 
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 (Pereira et al, 2000). 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 (Azzi et al., 2004).
[[Image:F1.large.jpg|left|frame|none|alt=Alt text|Figure 1. Structure of an AK in substrate-bound form<ref>http://www.pnas.org/content/95/15/8449/F1.large.jpg</ref>]]
== Application to the Animal Kingdom ==
 
Arginine Kinase is the individual phosphagen kinase that is found in major invertebrates, such as: arthropods, molluscs, and echinoderms. Most recently, an arginine kinase was purified from a house fly and a crystalline preparation was obtained from the thorax of a honey bee. This gave Wallimann and Eppenberger the initiative to investigate the arginine kinase in Drosophila melanogaster. Since the genome and genetic development of Drosophila melanogaster is well understood, this allows for any discoveries made to be easily interpreted. Additionally, further discoveries will help better understand the characteristics of arginine kinase corresponding vertebrate enzyme, creatine kinase (Wallimann et al., 1973)
[[Image:3M10 bio r 500.jpg|inline|left|frame|none|alt=Alt text|Figure 2. Structure of an AK in an unbound conformation<ref>http://www.rcsb.org/pdb/explore.do?structureId=4GVZ</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 (Wang et al., 1998). In the study by Wang et al. 1998, a phylogenetic tree was put together for the evolution of Arginine Kinase compared to Creatine Kinase. It indicates that there are major clusters corresponding to Creatine Kinase and Arginine Kinase. In the Arginine Kinase cluster, grasshopper is more similar to Drosophila than to lobster or horseshoe crab. Also, it is expressed in the gills of two species of euryhaline crabs, the blue crab Callinectes sapidus and the shore crab Carcinus maenus, in which energy-requiring functions include monovalent ion transport, acid-base balance, nitrogen excretion (Kotylar et al. 2000).
Arginine Kinase is the major phosphagen kinase found in invertebrates.


This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


</StructureSection>
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
== References ==
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 (Figure 2) to aid in the increase of ATP’s affinity for the binding site <ref>DOI 10.1080/08927022.2011.561430</ref>. Typically two arginine kinase structures mirror each other and form a hole like structure in between the two (Figure 1).
<references/>
Azzi, A., Clark, S. A., Ellington, W. R., & Chapman, M. S. (2004). The role of
phosphagen specificity loops in arginine kinase. Protein Science : A Publication
of the Protein Society,13(3), 575–585. http://doi.org/10.1110/ps.03428304
   
Kotlyar, S., Weihrauch, D., Paulsen, R., & Towle, D. (2000, July 20). Expression of Arginine Kinase Enzymatic Activity and mRNA in Gills of the Euryhaline Crabs Carcinus Maenas and Callinectes Sapidus. Retrieved November 17, 2015, from http://jeb.biologists.org/content/jexbio/203/16/2395.full.pdf


Newsholme, E. A., Beis, I., Leech, A. R., & Zammit, V. A. (1978). The role of creatine
== Function ==
kinase and arginine kinase in muscle. Biochemical Journal, 172(3), 533–537.
Arginine Kinase is part of a class of kinases that regulates ATP levels in the body to help maintain homeostasis. Arginine Kinase is a phosphokinase - a kinase used in the catalyzation of phosphagens and adenosine diphosphate (ADP) into adenosine triphosphate (ATP). It creates a sort of storage option for energy.  Phosphagens act as a storage form of phosphate (Nω-phospho-L-arginine) that can be catalyzed into an energy source (ATP) when needed <ref name=pereira2000> Pereira, C. A., Alonso, G. D., Paveto, M. C., Iribarren, A., Cabanas, M. L., Torres, H. N.
Pereira, C. A., Alonso, G. D., Paveto, M. C., Iribarren, A., Cabanas, M. L., Torres, H. N.
& 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.
cloning., J. Biol.Chem. 275, 1495-1501.</ref>. The arginine kinase is a lock and key catalyst that holds ADP and phosphoarginine in place and catalyzes the transfer of phosphate from phosphoarginine to ADP forming arginine and ATP <ref>DOI 10.1110/ps.03428304</ref>.  It is the most common phosphokinase (PK) in invertebrates. The most common PK in vertebrates is Creatine Kinase <ref name =pereira2000 />


Strong, S., & Ellington, W. (1994). Isolation and sequence analysis of the gene for
== Application to the Animal Kingdom ==
arginine kinase from the chelicerate arthropod, Limulus polyphemus: Insights into
Arginine Kinase is the individual phosphagen kinase that is found in major invertebrates, such as: arthropods, mollusks, and echinoderms. Most recently, an arginine kinase was purified from a house fly <ref name=wallimann1973 />. This gave Wallimann and Eppenberger the initiative to investigate the arginine kinase in Drosophila melanogaster, also known as a fruit fly <ref name=wallimann1973 />. Since the genome and genetic development of Drosophila melanogaster is well understood, this allows for any discoveries made to be easily interpreted. Additionally, further discoveries will help better understand the characteristics of arginine kinase corresponding vertebrate enzyme, creatine kinase <ref name=wallimann1973 />.
catalytically important residues. Biochimica Et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 197-200.
 
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
(1998): 987-98. Web. 15 Nov. 2015. <http://www.jneurosci.org/content/18/3/987.full.pdf></ref>.  In the study by Wang et al. 1998, a phylogenetic tree was put together for the evolution of Arginine Kinase compared to Creatine Kinase.  It indicates that there are major clusters corresponding to Creatine Kinase and Arginine Kinase.  Also, it is expressed in the gills of two species of euryhaline crabs, the blue crab Callinectes sapidus and the shore crab Carcinus maenus, in which energy-requiring functions include monovalent ion transport, acid-base balance, nitrogen excretion <ref>Kotlyar, S., Weihrauch, D., Paulsen, R., & Towle, D. (2000, July 20). Expression of Arginine Kinase Enzymatic Activity and mRNA in Gills of the Euryhaline Crabs Carcinus Maenas and Callinectes Sapidus. Retrieved November 17, 2015, from http://jeb.biologists.org/content/jexbio/203/16/2395.full.pdf</ref>.


Wallimann, Theo, and Hans M. Eppenberger. "Properties of Arginine Kinase from
== References ==
Drosophila Melanogaster." Www.onlinelibrary.wiley.com. Laboratory of
Developmental Biology, Swiss Federal Institute of Technology, Zurich, 21 June 1973. Web. 12 Nov. 2015


Wang, Yu-mei E., Pia Esbensen, and David Bentley. "Arginine Kinase Expression and
<references/>
Localization in Growth Cone Migration." The Journal of Neuroscience 18.3
(1998): 987-98. Web. 15 Nov. 2015. <http://www.jneurosci.org/content/18/3/987.full.pdf>.
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