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Macrolide 2'-kinase

From Wikipedia, the free encyclopedia
macrolide 2'-kinase
Identifiers
EC no.2.7.1.136
CAS no.116036-69-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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

[edit]
  • 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. 41 (6). Tokyo: 823–7. doi:10.7164/antibiotics.41.823. PMID 3042731.