EC Number   |
General Information |
Reference |
|---|
   2.7.1.136 | evolution |
the macrolide phosphotransferase structures show that the enzymes are related to the aminoglycoside phosphotransferases, but are distinguished from them by the presence of a large interdomain linker that contributes to an expanded antibiotic binding pocket |
762485 |
| 2.7.1.136 | more |
the large interdomain linker contributes to an expanded antibiotic binding pocket. This pocket is largely hydrophobic, with a negatively charged patch located at a conserved aspartate residue. Comparison of the enzyme-macrolide complex structure with the structures of macrolides bound to their natural target, the 50S ribosome, overview. Nucleotides bind to MPH(2')-I in a cleft between the N-terminal lobe and the core subdomain of the C-terminal lobe, binding site structure analysis |
762485 |
| 2.7.1.136 | more |
the large interdomain linker contributes to an expanded antibiotic binding pocket. This pocket is largely hydrophobic, with a negatively charged patch located at a conserved aspartate residue. Comparison of the enzyme-macrolide complex structure with the structures of macrolides bound to their natural target, the 50S ribosome, overview. Nucleotides bind to MPH(2')-II in a cleft between the N-terminal lobe and the core subdomain of the C-terminal lobe, binding site structure analysis |
762485 |
| 2.7.1.136 | physiological function |
macrolide phosphotransferase enzymes can inactivate the macrolides, a class of antibiotic, characterized by a large macrocyclic lactone ring. Broad-spectrum resistance is conferred by the enzymes |
762485 |
