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Literature summary 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

Application

EC Number Application Comment Organism
3.4.16.4 medicine VanX, being a required enzyme for bacterial antibiotic resistance, should be a key target in circumventing clinical vancomycin resistance Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.13.22 expressed as a maltose-binding protein fusion protein in Escherichia coli Enterococcus faecium
3.4.16.4 into the pMAL-c2X vector for expression in Escherichia coli JM109 cells Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.13.22 D-Ala-PSI[P(OOH)O]-D-Ala
-
 Enterococcus faecium
3.4.13.22 D-Ala-PSI[P(OOH)O]-D-Phe
-
 Enterococcus faecium
3.4.16.4 D-Ala(P,O)D-Ala acts as slow binding inhibitor Escherichia coli
3.4.16.4 D-Ala(P,O)D-Phe acts as slow binding inhibitor Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.16.4 cell wall
-
 Escherichia coli 5618
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.16.4 Zn2+
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.16.4 24000
-
 determined by SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.16.4 D-Ala-D-Ala + H2O Escherichia coli
-
 D-Ala + D-Ala
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.13.22 Enterococcus faecium
-
-
-
3.4.16.4 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.13.22 by an amylose affinity column and further separation by the DEAE ion exchange chromatography Enterococcus faecium
3.4.16.4 using an amylose affinity column, the MBP-tag is removed by factor Xa cleavage Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.16.4 D-Ala-D-Ala + H2O
-
 Escherichia coli D-Ala + D-Ala
-
 ?
3.4.16.4 D-Ala-D-Phe + H2O
-
 Escherichia coli D-Ala + D-Phe
-
 ?
3.4.16.4 D-Ala-D-Trp + H2O
-
 Escherichia coli D-Ala + D-Trp
-
 ?
3.4.16.4 D-Ala-D-Tyr + H2O
-
 Escherichia coli D-Ala + D-Tyr
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.13.22 VanX
-
 Enterococcus faecium
3.4.16.4 D,D-dipeptidase
-
 Escherichia coli
3.4.16.4 serine-type D-Ala-D-Ala carboxypeptidase
-
 Escherichia coli
3.4.16.4 VanX
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.13.22 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
3.4.13.22 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