This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Arginine kinase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <StructureSection load=' | + | <StructureSection load='1bg0' size='340' side='right' caption='Arginine kinase complex with arginine (stick model) and ADP (PDB code [[4bg4]])' scene=''> |
| - | + | ||
== Function == | == Function == | ||
| - | The phosphagen kinase reaction of AK is central to cellular energy homeostasis, i.e. maintenance of ATP level in invertebrates. | + | '''Arginine kinase''' (AK) is a phosphagen kinase which catalyzes the conversion of L-arginine and ATP to N-phospho-L-arginine and ADP. AK is part of arginine and proline metabolism. The phosphagen kinase reaction of AK is central to cellular energy homeostasis, i.e. maintenance of ATP level in invertebrates. Another phosphagen kinase found mostly in vertebrates is [[Creatine Kinase]] whose substrate is creatine. |
== Disease == | == Disease == | ||
== Relevance == | == Relevance == | ||
| + | |||
| + | High levels of Arg are found in plasma of patients with chronic hemolytic anemia. | ||
== Structural highlights == | == Structural highlights == | ||
Revision as of 11:33, 3 November 2015
| |||||||||||
3D structures of arginine kinase
Updated on 03-November-2015
