| lombricine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.5 | ||||||||
| CAS no. | 9026-53-3 | ||||||||
| 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 lombricine kinase ( EC 2.7.3.5) is an enzyme that catalyzes the chemical reaction
- ATP + lombricine ADP + N-phospholombricine
The two substrates of this enzyme are ATP and lombricine, and the two products are ADP and N-phospholombricine.
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:lombricine N-phosphotransferase. This enzyme participates in glycine, serine and threonine metabolism.
References
- Gaffney TJ, Rosenberg H, Ennor AH (1964). "The purification and properties of adenosine triphosphate-lombricine phosphotransferase". Biochem. J. 90 (1): 170–6. 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.
- Pant R (1959). "Isolation of lombricine and its enzymatic phosphorylation". Biochem. J. 73: 30–33.
- 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.
| lombricine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.5 | ||||||||
| CAS no. | 9026-53-3 | ||||||||
| 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 lombricine kinase ( EC 2.7.3.5) is an enzyme that catalyzes the chemical reaction
- ATP + lombricine ADP + N-phospholombricine
The two substrates of this enzyme are ATP and lombricine, and the two products are ADP and N-phospholombricine.
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:lombricine N-phosphotransferase. This enzyme participates in glycine, serine and threonine metabolism.
References
- Gaffney TJ, Rosenberg H, Ennor AH (1964). "The purification and properties of adenosine triphosphate-lombricine phosphotransferase". Biochem. J. 90 (1): 170–6. 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.
- Pant R (1959). "Isolation of lombricine and its enzymatic phosphorylation". Biochem. J. 73: 30–33.
- 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.