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Literature summary for 3.4.16.4 extracted from

  • Sarkar, S.K.; Chowdhury, C.; Ghosh, A.S.
    Deletion of penicillin-binding protein 5 (PBP5) sensitises Escherichia coli cells to beta-lactam agents (2010), Int. J. Antimicrob. Agents, 35, 244-249.
    View publication on PubMed
Search for more literature for 3.4.16.4

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
amoxicillin
-
 Escherichia coli
ampicillin
-
 Escherichia coli
cefaclor
-
 Escherichia coli
cefadroxil
-
 Escherichia coli
cefalexin
-
 Escherichia coli
cefalothin
-
 Escherichia coli
penicillin G
-
 Escherichia coli
piperacillin
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 strains K-12 and 2443
-

Purification (Commentary)

Purification (Comment) Organism
ampicillin-affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
-
 Escherichia coli Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-alanine
-
 ?

Synonyms

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

General Information

General Information Comment Organism
malfunction loss of penicillin-binding protein 5 enhances beta-lactam susceptibility, the observed susceptibilities for ampicillin, piperacillin, amoxicillin, penicillin G, cefadroxil and cefalexin are enhanced by 4fold and for cefalothin and cefaclor the susceptibilities are at least 8fold higher in the mutants Escherichia coli