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Literature summary for 3.4.17.8 extracted from

  • Josephine, H.R.; Charlier, P.; Davies, C.; Nicholas, R.A.; Pratt, R.F.
    Reactivity of penicillin-binding proteins with peptidoglycan-mimetic beta-lactams: whats wrong with these enzymes? (2006), Biochemistry, 45, 15873-15883.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
(5R,6R)-6-[(7-ammonio-7-carboxylatoheptanoyl)amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylate
-
Escherichia coli
6-beta(D-alpha-aminopimelyl)-aminopenicillanic acid
-
Escherichia coli
6-beta(N-acetyl-L-alanyl-gamma-D-glutamyl-L-alanyl)-aminopenicillanic acid
-
Escherichia coli
7-beta(D-alpha-aminopimelyl)-aminocephalosporanic acid
-
Escherichia coli
benzylpenicillin
-
Escherichia coli
cephalothin
-
Escherichia coli
additional information synthesis and inhibitory potency of beta-lactam derivatives, overview Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
gene pbp5
-

Synonyms

Synonyms Comment Organism
DD-peptidase
-
Escherichia coli
PBP5
-
Escherichia coli
penicillin-binding protein 5
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information
-
Escherichia coli