| guanidinoacetate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.1 | ||||||||
| CAS no. | 9026-60-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a guanidinoacetate kinase ( EC 2.7.3.1) is an enzyme that catalyzes the chemical reaction
- ATP + guanidinoacetate ADP + phosphoguanidinoacetate
Thus, the two substrates of this enzyme are ATP and guanidinoacetate, whereas its two products are ADP and phosphoguanidinoacetate.
Guanidinoacetate kinase belongs to the family of transferases, specifically those that transfer phosphorus-containing groups ( phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:guanidinoacetate N-phosphotransferase. This enzyme is also called glycocyamine kinase. This enzyme participates in arginine and proline metabolism.
- HOBSON GE, REES KR (1957). "The annelid phosphokinases". Biochem. J. 65 (2): 305–7. PMC 1199870. PMID 13403909.
- Pradel LA; Kassab R; Conlay C; Nguyen Van Thoai (1968). "[Properties and amino acid composition of purified ATP: guanidinoacetate phosphotransferase]". Biochim. Biophys. Acta. 154 (2): 305–14. doi: 10.1016/0005-2795(68)90044-5. PMID 5637051.
- Pradel LA, Kassab R, Thoai NV (1964). "Sur l'acide adenosine-triphosphorique:guanidoacetate phosphotransferase". Biochim. Biophys. Acta. 81: 86–95. doi: 10.1016/0926-6569(64)90338-4.
- Thoai NV (1957). "Sur la taurocyamine et la glycocyamine phosphokinase". Bull. Soc. Chim. Biol. 39: 197–208.
| guanidinoacetate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.1 | ||||||||
| CAS no. | 9026-60-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a guanidinoacetate kinase ( EC 2.7.3.1) is an enzyme that catalyzes the chemical reaction
- ATP + guanidinoacetate ADP + phosphoguanidinoacetate
Thus, the two substrates of this enzyme are ATP and guanidinoacetate, whereas its two products are ADP and phosphoguanidinoacetate.
Guanidinoacetate kinase belongs to the family of transferases, specifically those that transfer phosphorus-containing groups ( phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:guanidinoacetate N-phosphotransferase. This enzyme is also called glycocyamine kinase. This enzyme participates in arginine and proline metabolism.
- HOBSON GE, REES KR (1957). "The annelid phosphokinases". Biochem. J. 65 (2): 305–7. PMC 1199870. PMID 13403909.
- Pradel LA; Kassab R; Conlay C; Nguyen Van Thoai (1968). "[Properties and amino acid composition of purified ATP: guanidinoacetate phosphotransferase]". Biochim. Biophys. Acta. 154 (2): 305–14. doi: 10.1016/0005-2795(68)90044-5. PMID 5637051.
- Pradel LA, Kassab R, Thoai NV (1964). "Sur l'acide adenosine-triphosphorique:guanidoacetate phosphotransferase". Biochim. Biophys. Acta. 81: 86–95. doi: 10.1016/0926-6569(64)90338-4.
- Thoai NV (1957). "Sur la taurocyamine et la glycocyamine phosphokinase". Bull. Soc. Chim. Biol. 39: 197–208.