Macrolide 2'-kinase
In enzymology, a macrolide 2'-kinase (EC 2.7.1.136) is an enzyme that catalyzes the chemical reaction
- ATP + oleandomycin ADP + oleandomycin 2'-O-phosphate
| macrolide 2'-kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.1.136 | ||||||||
| CAS number | 116036-69-2 | ||||||||
| 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 | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are ATP and oleandomycin, whereas its two products are ADP and oleandomycin 2'-O-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:macrolide 2'-O-phosphotransferase.
References
- O'Hara K, Kanda T, Kono M (June 1988). "Structure of a phosphorylated derivative of oleandomycin, obtained by reaction of oleandomycin with an extract of an erythromycin-resistant strain of Escherichia coli". J. Antibiot. Tokyo. 41 (6): 823–7. doi:10.7164/antibiotics.41.823. PMID 3042731.
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