Cloned (Comment) | Organism |
---|---|
expressed as a maltose-binding protein fusion protein in Escherichia coli | Enterococcus faecium |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
D-Ala-PSI[P(OOH)O]-D-Ala | - |
Enterococcus faecium | |
D-Ala-PSI[P(OOH)O]-D-Phe | - |
Enterococcus faecium |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Enterococcus faecium | - |
- |
- |
Purification (Comment) | Organism |
---|---|
by an amylose affinity column and further separation by the DEAE ion exchange chromatography | Enterococcus faecium |
Synonyms | Comment | Organism |
---|---|---|
VanX | - |
Enterococcus faecium |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00196 | - |
D-Ala-PSI[P(OOH)O]-D-Phe | koff: 0.00231 sec-1, results reveals that both dipeptide phosphonates are slow-binding inhibitors of VanX. Moreover, in comparison with D-Ala(P,O)D-Ala phosphonate dipeptide, an additional aromatic interaction with the Phe79 residue in the active site of the enzyme may account for its higher affinity to VanX | Enterococcus faecium | |
0.0165 | - |
D-Ala-PSI[P(OOH)O]-D-Ala | koff: 0.0180 sec-1, results reveals that both dipeptide phosphonates are slow-binding inhibitors of VanX | Enterococcus faecium |