Taurocyamine kinase
| Taurocyamine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.4 | ||||||||
| CAS no. | 9026-72-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Taurocyamine kinase (EC 2.7.3.4) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from from several species of polychaete worms converts taurocyamine to N-phosphotaurocyamine by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The reaction is part of the metabolism of taurine and hypotaurine.[1][2][3][4]
This enzyme is a transferase, specifically one 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.[5]
References
- ↑ Hobson GE, Rees KR (1957). "The annelid phosphokinases". Biochem. J. 65 (2): 305–7. doi:10.1042/bj0650305. 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. PMID 14068521.
- ↑ Enzyme 2.7.3.4 at KEGG Pathway Database.
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