Lombricine kinase
| Lombricine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.5 | ||||||||
| CAS no. | 9026-53-3 | ||||||||
| 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 | ||||||||
| |||||||||
Lombricine kinase (EC 2.7.3.5) is an enzyme that catalyzes the chemical reaction
The enzyme first characterised from the worm species, Lumbricus terrestris, converts the phosphagen,[1] lombricine, to N-phospholombricine by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[2] The enzyme is found widely in annelids, where D-lombricine is the favoured form but some marine worms (echiuroids) contain L-lombricine derived from L-serine.[3][4][5][6] The enzyme is one of a group of phosphagen kinases that includes hypotaurocyamine kinase.[7]
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:lombricine N-phosphotransferase.[8]
References
- ↑ 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.
- ↑ Pant R (1959). "Isolation of lombricine and its enzymatic phosphorylation". Biochem. J. 73: 30–33. doi:10.1042/bj0730030. PMC 1197007. PMID 14430183.
- ↑ Gaffney TJ, Rosenberg H, Ennor AH (1964). "The purification and properties of adenosine triphosphate-lombricine phosphotransferase". Biochem. J. 90 (1): 170–6. doi:10.1042/bj0900170. PMC 1202539. PMID 5832288.
- ↑ Kassab R; Pradel LA; Nguyen Van Thoai (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.
- ↑ van Thoai N, Robin Y, Guillou Y (1972). "A new phosphagen, N'-phosphorylguanidinoethylphospho-O-( -N,N-dimethyl)serine (phosphothalassemine)". Biochemistry. 11 (21): 3890–5. doi:10.1021/bi00771a009. PMID 5079888.
- ↑ Petkowski, Janusz J.; Bains, William; Seager, Sara (2019). "Natural Products Containing 'Rare' Organophosphorus Functional Groups". Molecules. 24 (5): 866. doi:10.3390/molecules24050866. PMC 6429109. PMID 30823503.
- ↑ 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.
- ↑ Enzyme 2.7.3.5 at KEGG Pathway Database.