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 3: | Line 3: | ||
== Function == | == Function == | ||
| - | '''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. | + | '''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. <ref>PMID:25849389</ref> Another phosphagen kinase found mostly in vertebrates is [[Creatine Kinase]] whose substrate is creatine. |
== Relevance == | == Relevance == | ||
Revision as of 09:38, 8 December 2015
| |||||||||||
3D structures of arginine kinase
Updated on 08-December-2015
References
- ↑ Wang Z, Qiao Z, Ye S, Zhang R. Structure of a double-domain phosphagen kinase reveals an asymmetric arrangement of the tandem domains. Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):779-89. doi:, 10.1107/S1399004715001169. Epub 2015 Mar 26. PMID:25849389 doi:http://dx.doi.org/10.1107/S1399004715001169
- ↑ Zhou G, Somasundaram T, Blanc E, Parthasarathy G, Ellington WR, Chapman MS. Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions. Proc Natl Acad Sci U S A. 1998 Jul 21;95(15):8449-54. PMID:9671698
