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. <ref>PMID:25849389</ref> Another phosphagen kinase found mostly in vertebrates is [[Creatine Kinase]] whose substrate is creatine. | + | '''Arginine kinase''' or '''Protein-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. |
For more details see [[Arginine Kinase AK]]. | For more details see [[Arginine Kinase AK]]. | ||
Current revision
| |||||||||||
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
