Adenylate kinase
| Adenylate kinase 1 | |||||||
|---|---|---|---|---|---|---|---|
 3D ribbon/surface model of adenylate kinase in complex with bis(adenosine)teraphosphate (ADP-ADP) | |||||||
| Identifiers | |||||||
| Symbol | AK1 | ||||||
| NCBI gene | 203 | ||||||
| HGNC | 361 | ||||||
| OMIM | 103000 | ||||||
| PDB | 2c95 | ||||||
| RefSeq | NM_000476 | ||||||
| UniProt | P00568 | ||||||
| Other data | |||||||
| EC number | 2.7.4.3 | ||||||
| Locus | Chr. 9 q34.1 | ||||||
| |||||||
Adenylate kinase (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides, and plays an important role in cellular energy homeostasis (see the "Biological homeostasis" section of "Homeostasis"). The reaction catalyzed is:
The equilibrium constant in the direction written is 0.44. Thus, the ΔGo for this reaction is close to zero. In muscle of a variety of species of vertebrates and invertebrates, the concentration of ATP is typically 7-10 times that of ADP, and usually greater than 100 times that of AMP [1]. The rate of oxidative phosphorylation is controlled by the availability of ADP. Thus, the mitochondrion attempts to keep ATP levels high due to the combined action of adenylate kinase and the controls on oxidative phosphorylation.
References
- ^ Beis I., and Newsholme E. A. (1975). The contents of adenine nucleotides, phosphagens and some glycolytic intermediates in resting muscles from vertebrates and invertebrates. Biochem J 152, 23-32.
External links
- Adenylate+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)