EC Number |
Inhibitors |
Structure |
---|
2.7.1.190 | apramycin |
- |
|
2.7.1.190 | butirosin |
- |
|
2.7.1.190 | butirosin A/B |
- |
|
2.7.1.190 | kanamycin A |
- |
|
2.7.1.190 | lividomycin A |
- |
|
2.7.1.190 | more |
the ternary complex between APH(2'')-IIIa, GDP and kanamycin can be regarded as an inactive abortive complex, since the gamma-phosphate group which would normally be transferred to the 2''-hydroxyl of the substrate is absent. The cofactor binding in the ternary complex is similar in detail to that in the previously described binary complex |
|
2.7.1.190 | more |
identification os specific inhibitors of APHs that can restore bacterial susceptibility to aminoglycosides, screening of the Zinc database for search for allosteric inhibitors that bind to small cavities of the protein and block the enzyme function by perturbing its dynamics, docking study usig the crystal structure of the enzyme (PDB ID 3SG8) with removed aminoglycoside substrate, overview. The two interactions with side chain of Arg211 and backbones of Leu209 and Gly210 are shown to play an essential role in the inhibition of APH. No inhibition by ZINC6751595 and ZINC8981627 |
|
2.7.1.190 | more |
inhibitor screening of a chemical library using ultra-high performance liquid chromatography-quadrupole-time-of-flight mass spectrometry, assay method optimization and validation, overview. Poor inhibition by Mer-C-3, Mer-C-8e, and paromomycin |
|
2.7.1.190 | neamine |
- |
|
2.7.1.190 | neomycin |
- |
|