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Literature summary for 3.4.13.22 extracted from

  • Chang, Y.P.; Tseng, M.J.; Chu, Y.H.
    Using surface plasmon resonance to directly measure slow binding of low-molecular mass inhibitors to a VanX chip (2006), Anal. Biochem., 359, 63-71.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed as a maltose-binding protein fusion protein in Escherichia coli Enterococcus faecium

Inhibitors

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

Organism UniProt Comment Textmining
Enterococcus faecium
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by an amylose affinity column and further separation by the DEAE ion exchange chromatography Enterococcus faecium

Synonyms

Synonyms Comment Organism
VanX
-
Enterococcus faecium

Ki Value [mM]

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