| taurocyamine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.4 | ||||||||
| CAS no. | 9026-72-6 | ||||||||
| 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 taurocyamine kinase (EC 2.7.3.4) is an enzyme that catalyzes the chemical reaction
- ATP + taurocyamine ADP + N-phosphotaurocyamine
Thus, the two substrates of this enzyme are ATP and taurocyamine, whereas its two products are ADP and N-phosphotaurocyamine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:taurocyamine N-phosphotransferase. Other names in common use include taurocyamine phosphotransferase, and ATP:taurocyamine phosphotransferase. This enzyme participates in taurine and hypotaurine metabolism.
References
- HOBSON GE, REES KR (1957). "The annelid phosphokinases". Biochem. J. 65 (2): 305–7. PMC 1199870. PMID 13403909.
- Kassab R, Pradel LA, Nguyen VT (1965). "[ATP:taurocyamine and ATP:lombricine phosphotransferases Purification and study of SH groups]". Biochim. Biophys. Acta. 99 (3): 397–405. doi:10.1016/s0926-6593(65)80194-1. PMID 5840960.
- Thoai NV (1957). "Sur la taurocyamine et la glycocyamine phosphokinase". Bull. Soc. Chim. Biol. 39: 197–208.
- Thoai NV, Robin Y, Pradel L-A (1963). "Hypotaurocyamine phosphokinase comparison avec la taurocyamine phosphokinase". Biochim. Biophys. Acta. 73 (3): 437–444. doi:10.1016/0006-3002(63)90445-1.
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