Macrolide 2'-kinase

From Wikipedia, the free encyclopedia

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.

[edit] References

• IUBMB entry for 2.7.1.136
• BRENDA references for 2.7.1.136 (Recommended.)
• PubMed references for 2.7.1.136
• PubMed Central references for 2.7.1.136
• Google Scholar references for 2.7.1.136
• O'Hara K, Kanda T, Kono M (Tokyo). "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.: 823–7. PMID 3042731. 

[edit] External links

The CAS registry number for this enzyme class is 116036-69-2.

• IUBMB entry for 2.7.1.136

• KEGG entry for 2.7.1.136

• BRENDA entry for 2.7.1.136

• NiceZyme view of 2.7.1.136

• EC2PDB: PDB structures for 2.7.1.136

• PRIAM entry for 2.7.1.136

• PUMA2 entry for 2.7.1.136

• IntEnz: Integrated Enzyme entry for 2.7.1.136

• MetaCyc entry for 2.7.1.136

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0050073: macrolide 2'-kinase

• AMIGO entry for GO code 0050073: macrolide 2'-kinase