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Literature summary for 3.4.17.8 extracted from

  • Cremniter, J.; Mainardi, J.; Josseaume, N.; Quincampoix, J.; Dubost, L.; Hugonnet, J.; Marie, A.; Gutmann, L.; Rice, L.B.; Arthur, M.
    Novel mechanism of resistance to glycopeptide antibiotics in Enterococcus faecium (2006), J. Biol. Chem., 281, 32254-32262.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.17.8

Protein Variants

Protein Variants Comment Organism
D344S the mutant shows highly reduced activity compared to the wild-type Enterococcus faecium
additional information construction of spontaneous mutants M512, M9, and G9 from mutant D344S with reduced enzyme activity, but less as for the parental mutant D344S, overview Enterococcus faecium

Inhibitors

Inhibitors Comment Organism Structure
ampicillin inhibits the D,D-carboxypeptidase activity of penicillin-binding proteins Enterococcus faecium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Enterococcus faecium activation of the L,D-transpeptidation pathway can also release inhibition of transglycosylation, leading to cross-resistance to glycopeptides and beta-lactams following extensive hydrolysis of D-Ala5 from the cytoplasmic precursor UDP-MurNAc-pentapeptide by a D,D-carboxypeptidase, mechanism of glycopeptide resistance, overview ?
-
 ?
UDP-MurNAc-pentapeptide + H2O Enterococcus faecium i.e. UDP-acetylmuramic acid-L-Ala-D-iGlu-L-Lys-D-Ala-D-Ala UDP-MurNAc-tetrapeptide + D-Ala
-
 ?

Organism

Organism UniProt Comment Textmining
Enterococcus faecium
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-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0076
-
 mutant D344S Enterococcus faecium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala + H2O D,D-carboxypeptidase activity of penicillin-binding proteins Enterococcus faecium L-Ala-D-gamma-Glu-L-Lys-D-Ala + D-Ala
-
 ?
additional information activation of the L,D-transpeptidation pathway can also release inhibition of transglycosylation, leading to cross-resistance to glycopeptides and beta-lactams following extensive hydrolysis of D-Ala5 from the cytoplasmic precursor UDP-MurNAc-pentapeptide by a D,D-carboxypeptidase, mechanism of glycopeptide resistance, overview Enterococcus faecium ?
-
 ?
UDP-MurNAc-pentapeptide + H2O i.e. UDP-acetylmuramic acid-L-Ala-D-iGlu-L-Lys-D-Ala-D-Ala Enterococcus faecium UDP-MurNAc-tetrapeptide + D-Ala
-
 ?
UDP-MurNAc-pentapeptide + H2O i.e. UDP-N-acetylmuramic acid-L-Ala-D-iGlu-L-Lys-D-Ala-D-Ala Enterococcus faecium UDP-MurNAc-tetrapeptide + D-Ala
-
 ?