Adenylate kinase
| Adenylate kinase | ||
|---|---|---|
|
||
| Ribbon / surface model with P1, P4-Di (adenosine-5 ′) tetraphosphate (ADP-ADP) according to PDB 2C95 . Active center (green), ADP binding site (yellow) | ||
| Properties of human protein | ||
| Mass / length primary structure | 194 amino acids | |
| Secondary to quaternary structure | Monomer | |
| Identifier | ||
| Gene name | AK1 | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 2.7.4.3 , kinase | |
| Response type | (De-) phosphorylation | |
| Substrate | ATP + AMP | |
| Products | ADP + ADP | |
The enzyme adenylate kinase (AK1) (also myokinase and AMP kinase ) catalyzes the following reactions in order to maintain the balance between the phosphate acceptor ADP and the phosphate donor ATP :
- 2 ADP → ATP + AMP
Subsequently, the hydrolysis of the ATP releases energy, which can be used in muscles or other tissues.
The reaction is also possible in the other direction if there is excess ATP and ADP is necessary as an energy store:
- ATP + AMP → 2 ADP
At least three isoforms of the enzyme have developed in mammals ; five alleles are known in humans . The oldest form can also be found in other living things, with the exception of the archaea . In humans it is localized in all types of tissue. Adenylate kinase deficiency caused by mutation in the AK1 gene leads to a form of hemolytic anemia .
Web links
Individual evidence
- ↑ Swiss Institute of Bioinformatics (SIB): PROSITE documentation PDOC00104. Adenylate kinase. Retrieved September 20, 2011 .
- ↑ UniProt P00568