In enzymology, a nucleoside-triphosphate-adenylate kinase (EC 2.7.4.10) is an enzyme that catalyzes the chemical reaction
| nucleoside triphosphate adenylate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.4.10 | ||||||||
| CAS no. | 9026-74-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- nucleoside triphosphate + AMP nucleoside diphosphate + ADP
Thus, the two substrates of this enzyme are nucleoside triphosphate and AMP, whereas its two products are nucleoside diphosphate and ADP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is nucleoside-triphosphate:AMP phosphotransferase. Other names in common use include guanosine triphosphate-adenylate kinase, nucleoside triphosphate-adenosine monophosphate transphosphorylase, GTP:AMP phosphotransferase, and isozyme 3 of adenylate kinase. This enzyme participates in pyrimidine metabolism.
Structural studies
editAs of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1ZD8 and 2AK3.
References
edit- Albrecht GJ (1970). "Purification and properties of nucleoside triphosphate-adenosine monophosphate transphosphorylase from beef heart mitochondria". Biochemistry. 9 (12): 2462–70. doi:10.1021/bi00814a011. PMID 5423264.
- CHIGA M, ROGERS AE, PLAUT GW (1961). "Nucleotide transphosphorylases from liver. II. Purification and properties of a 6-oxypurine nucleoside triphosphate-adenosine monophosphate transphosphorylase from swine liver". J. Biol. Chem. 236 (6): 1800–5. doi:10.1016/S0021-9258(19)63306-5. PMID 13693071.
