Literature summary for 3.4.16.4 extracted from

Sauvage, E.; Herman, R.; Petrella, S.; Duez, C.; Bouillenne, F.; Fr�re, J.M.; Charlier, P.
Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins (2005), J. Biol. Chem., 280, 31249-31256.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Actinomadura sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
by hanging drop vapor diffusion, at 1.8 A and 2.4 A resolution, R39 structure is composed of one penicillin binding domain and two unknown domains, the R39 active site does not undergo a great structural deformation upon beta-lactam binding	Actinomadura sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
beta-lactam	R39 has a high beta-lactam binding activity	Actinomadura sp.

Organism

Organism	UniProt	Comment	Textmining
Actinomadura sp.	-	-	-
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Actinomadura sp.

Synonyms

Synonyms	Comment	Organism
DD-peptidase	-	Escherichia coli
DD-peptidase	-	Actinomadura sp.
PBP	-	Actinomadura sp.
PBP5	-	Escherichia coli
penicillin-binding protein	-	Escherichia coli
penicillin-binding protein	-	Actinomadura sp.

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Release 2023.1 (January 2023)