User:Michael Adams/Sandbox 1: Difference between revisions
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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 | 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 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). | ||
== Function == | == Function == | ||
