User:Michael Adams/Sandbox 1: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 9: | Line 9: | ||
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. | 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. | ||
== Structure == | == Structure == | ||
The structure of arginine kinase is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding. (Figure 1b). 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 β-sheet with seven α-helices flanking the sheet ( | The structure of arginine kinase is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding. (Figure 1b). 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 β-sheet with seven α-helices flanking the sheet Copy and paste the following line where you want the scene link to appear (scroll down if needed) and edit the TextToBeDisplayed: | ||
[[Image:F1.large.jpg | <scene name='71/716599/Mynewscene/1'>TextToBeDisplayed</scene> (Figure 1). | ||
[[Image:F1.large.jpg]][[Image:3M10 bio r 500.jpg]] | |||
Figure 1a (Left). Structure of an arginine kinase in substrate-bound form Figure 1b (right). Structure of an AK in an unbound conformation. | Figure 1a (Left). Structure of an arginine kinase in substrate-bound form Figure 1b (right). Structure of an AK in an unbound conformation. | ||
ATP + L-arginine ADP + Nω-phospho-L-arginine | ATP + L-arginine ADP + Nω-phospho-L-arginine | ||
| Line 26: | Line 27: | ||
== Application to the Animal Kingdom == | == Application to the Animal Kingdom == | ||
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 | 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 (Walliman et al. 1973). 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 />. | ||
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 | ||
