User:Michael Adams/Sandbox 1: Difference between revisions
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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== | ||
A phosphokinase used to store energy in the form of Argininephosphate. | A phosphokinase used to store energy in the form of Argininephosphate. | ||
== Isolation Methods == | == Isolation Methods == | ||
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 <ref>DOI 10.1002/pro.5560060222</ref>. | 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 <ref>DOI 10.1002/pro.5560060222</ref>. | ||
== Structural | == 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 | ||
