Macrolide 2'-kinase
macrolide 2'-kinase | |||||||||
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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 / EGO | ||||||||
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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
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. "Structure of a phosphorylated derivative of oleandomycin, obtained by reaction of oleandomycin with an extract of an erythromycin-resistant strain of Escherichia coli". J. Tokyo. Antibiot. (6): 823–7. PMID 3042731.
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