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Literature summary for 3.4.16.4 extracted from

  • Reynolds, P.E.; Ambur, O.H.; Casadewall, B.; Courvalin, P.
    The VanY(D) DD-carboxypeptidase of Enterococcus faecium BM4339 is a penicillin-binding protein (2001), Microbiology, 147, 2571-2578.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
benzylpenicillin IC50: 0.00002 mg/ml, inhibition of the enzyme influences production of peptidoglycan precursors internally Enterococcus faecium

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound, the active site is present on the outside surface of the membrane Enterococcus faecium 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O Enterococcus faecium
-
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala + D-Ala
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O Enterococcus faecium BM4339
-
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala + D-Ala
-
?

Organism

Organism UniProt Comment Textmining
Enterococcus faecium
-
BM4339
-
Enterococcus faecium BM4339
-
BM4339
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information penicillin-binding protein Enterococcus faecium ?
-
?
additional information penicillin-binding protein Enterococcus faecium BM4339 ?
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O
-
Enterococcus faecium UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala + D-Ala
-
?
UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala + H2O
-
Enterococcus faecium BM4339 UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala + D-Ala
-
?

Synonyms

Synonyms Comment Organism
VanY(D) DD-carboxypeptidase
-
Enterococcus faecium
VanYD
-
Enterococcus faecium