Literature summary for 3.4.16.4 extracted from

Lavollay, M.; Arthur, M.; Fourgeaud, M.; Dubost, L.; Marie, A.; Riegel, P.; Gutmann, L.; Mainardi, J.L.
The beta-lactam-sensitive D,D-carboxypeptidase activity of Pbp4 controls the L,D and D,D transpeptidation pathways in Corynebacterium jeikeium (2009), Mol. Microbiol., 74, 650-661.

Search for more literature for 3.4.16.4

Cloned(Commentary)

Cloned (Comment)	Organism
a soluble fragment of Pbp4 lacking the putative membrane anchor of the protein is expressed in Escherichia coli	Corynebacterium jeikeium

Inhibitors

Inhibitors	Comment	Organism	Structure
ampicillin	complete inhibition at 0.57 mM, 95% inhibition at 0.285 mM	Corynebacterium jeikeium

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium jeikeium	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GlcNAc-MurNAc-L-Ala-D-iGluNH2-meso-diaminopimelic acid-NH2-D-Ala-D-Ala + H2O	-	Corynebacterium jeikeium	GlcNAc-MurNAc-L-Ala-D-iGluNH2-meso-diaminopimelic acid-NH2-D-Ala + D-Ala	-	?
additional information	the enzyme cleaves the C-terminal D-Ala5 of stem pentapeptides and forms the essential tetrapeptide substrate of a beta-lactam-insensitive L,D-transpeptidase	Corynebacterium jeikeium	?	-	?

Synonyms

Synonyms	Comment	Organism
D,D-carboxypeptidase	-	Corynebacterium jeikeium
PBP4	-	Corynebacterium jeikeium
penicillin-binding protein	-	Corynebacterium jeikeium

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.06	-	-	Corynebacterium jeikeium	ampicillin

General Information

General Information	Comment	Organism
physiological function	the beta-lactam-sensitive D,D-carboxypeptidase activity of Pbp4 controls the L,D and D,D transpeptidation pathways in Corynebacterium jeikeium	Corynebacterium jeikeium

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Release 2023.1 (January 2023)