Hypotaurocyamine kinase
| Hypotaurocyamine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.6 | ||||||||
| CAS no. | 9026-57-7 | ||||||||
| 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 | ||||||||
| |||||||||
Hypotaurocyamine kinase (EC 2.7.3.6) is an enzyme that catalyzes the reversible chemical reaction
The enzyme characterised from sipunculid worms converts hypotaurocyamine to N-phosphohypotaurocyamine by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2] There is evidence that the gene encoding this enzyme evolved from one coding for arginine kinase.[3][4] The reaction is reversible for the phosphagen product.[5]
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:hypotaurocyamine N-phosphotransferase.[6]
References
- ↑ Thoai NV, Robin Y, Pradel LA (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.
- ↑ Ellington, W Ross (2001). "Evolution and Physiological Roles of Phosphagen Systems". Annual Review of Physiology. 63: 289–325. doi:10.1146/annurev.physiol.63.1.289. PMID 11181958.
- ↑ Uda, Kouji; Iwai, Aki; Suzuki, Tomohiko (2005). "Hypotaurocyamine kinase evolved from a gene for arginine kinase". FEBS Letters. 579 (30): 6756–6762. doi:10.1016/j.febslet.2005.11.006. PMID 16325813.
- ↑ Tanaka, Kumiko; Uda, Kouji; Shimada, Mayumi; Takahashi, Ken-Ichi; Gamou, Shinobu; Ellington, W. Ross; Suzuki, Tomohiko (2007). "Evolution of the Cytoplasmic and Mitochondrial Phosphagen Kinases Unique to Annelid Groups". Journal of Molecular Evolution. 65 (5): 616–625. doi:10.1007/s00239-007-9046-4. PMID 17932618.
- ↑ Palmer, Allyson; Begres, Brittany N.; Van Houten, Jason M.; Snider, Mark J.; Fraga, Dean (2013). "Characterization of a putative oomycete taurocyamine kinase: Implications for the evolution of the phosphagen kinase family". Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 166 (3–4): 173–181. doi:10.1016/j.cbpb.2013.08.003. PMID 23978736.
- ↑ Enzyme 2.7.3.6 at KEGG Pathway Database.