| hamamelose kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.102 | ||||||||
| CAS no. | 74506-53-9 | ||||||||
| 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 hamamelose kinase ( EC 2.7.1.102) is an enzyme that catalyzes the chemical reaction
- ATP + D-hamamelose ADP + D-hamamelose 2'-phosphate
Thus, the two substrates of this enzyme are ATP and D-hamamelose, whereas its two products are ADP and D-hamamelose 2'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups ( phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-hamamelose 2'-phosphotransferase. Other names in common use include hamamelose kinase (phosphorylating), hamamelosekinase (ATP: hamamelose 2'-phosphotransferase), and ATP/hamamelose 2'-phosphotransferase.
References
- Beck E, Wieczorek J, Reinecke W (1980). "Purification and properties of hamamelosekinase". Eur. J. Biochem. 107 (2): 485–9. doi: 10.1111/j.1432-1033.1980.tb06054.x. PMID 6249593.
