EC Number   |
General Information |
Reference |
|---|
  2.1.1.237 | evolution |
structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases, overview |
735344 |
| 2.1.1.237 | malfunction |
construction of a MycF disrupion mutant. The disruption mutant mainly produces mycinamicin III |
715054 |
| 2.1.1.237 | metabolism |
the 3'-O-methyltransferase enzyme is involved in the biosynthesis of the macrolide antibiotic mycinamicin |
735344 |
| 2.1.1.237 | more |
using the MycF substrate complex and the modeled substrate complex of a 4'-specific homologue, active site residues were identified that correlate with the 3' or 4' specificity of MycF family members and define the protein and substrate features that direct the regiochemistry of methyltransfer |
735344 |
| 2.1.1.237 | physiological function |
S-adenosyl-L-methionine cofacor binding induces substantial ordering that creates the binding site for the natural substrate, and a bound metal ion positions the substrate for catalysis |
735344 |
| 2.1.1.237 | physiological function |
the enzyme is involved in the biosynthesis of mycinamicin macrolide antibiotics. Mycinamicins represent a family of macrolide antibiotics with more than twenty members produced by the rare actinomycete Micromonospora griseorubida |
714732 |
