Literature summary for 3.4.16.4 extracted from

Pratt, R.F.
Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins) (2008), Cell. Mol. Life Sci., 65, 2138-2155.

Application

Application	Comment	Organism
medicine	bacterial DD-peptidases are still an enticing target for antibacterial agents	Staphylococcus aureus
medicine	bacterial DD-peptidases are still an enticing target for antibacterial agents	Haemophilus influenzae
medicine	bacterial DD-peptidases are still an enticing target for antibacterial agents	Bacillus subtilis
medicine	bacterial DD-peptidases are still an enticing target for antibacterial agents	Escherichia coli
medicine	bacterial DD-peptidases are still an enticing target for antibacterial agents	Neisseria gonorrhoeae
medicine	bacterial DD-peptidases are still an enticing target for antibacterial agents	Streptococcus pneumoniae
medicine	bacterial DD-peptidases are still an enticing target for antibacterial agents	Streptomyces sp.
medicine	bacterial DD-peptidases are still an enticing target for antibacterial agents	Caulobacter vibrioides
medicine	bacterial DD-peptidases are still an enticing target for antibacterial agents	Streptomyces sp. R61
medicine	bacterial DD-peptidases are still an enticing target for antibacterial agents	Streptomyces sp. K15

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Bacillus subtilis
-	Escherichia coli
-	Streptomyces sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
beta-lactam	-	Streptomyces sp.
Moenomycin	-	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Escherichia coli	16020	-
membrane	-	Streptococcus pneumoniae	16020	-

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-
Caulobacter vibrioides	-	-	-
Escherichia coli	-	-	-
Haemophilus influenzae	-	-	-
Neisseria gonorrhoeae	-	-	-
Staphylococcus aureus	-	-	-
Streptococcus pneumoniae	-	-	-
Streptomyces sp.	-	-	-
Streptomyces sp. K15	-	-	-
Streptomyces sp. R61	-	-	-

Synonyms

Synonyms	Comment	Organism
D-alanyl-D-alanine transpeptidase	-	Staphylococcus aureus
D-alanyl-D-alanine transpeptidase	-	Haemophilus influenzae
D-alanyl-D-alanine transpeptidase	-	Bacillus subtilis
D-alanyl-D-alanine transpeptidase	-	Escherichia coli
D-alanyl-D-alanine transpeptidase	-	Neisseria gonorrhoeae
D-alanyl-D-alanine transpeptidase	-	Streptococcus pneumoniae
D-alanyl-D-alanine transpeptidase	-	Streptomyces sp.
D-alanyl-D-alanine transpeptidase	-	Caulobacter vibrioides
D-alanyl-D-alanine transpeptidase	-	Streptomyces sp. R61
D-alanyl-D-alanine transpeptidase	-	Streptomyces sp. K15
DD-peptidase	-	Staphylococcus aureus
DD-peptidase	-	Haemophilus influenzae
DD-peptidase	-	Bacillus subtilis
DD-peptidase	-	Escherichia coli
DD-peptidase	-	Neisseria gonorrhoeae
DD-peptidase	-	Streptococcus pneumoniae
DD-peptidase	-	Streptomyces sp.
DD-peptidase	-	Caulobacter vibrioides
DD-peptidase	-	Streptomyces sp. R61
DD-peptidase	-	Streptomyces sp. K15
PBP1a	-	Escherichia coli
PBP1b	-	Escherichia coli
PBP3	-	Neisseria gonorrhoeae
PBP3	-	Streptococcus pneumoniae
PBP4	-	Escherichia coli
PBP4a	-	Bacillus subtilis
PBP5	-	Escherichia coli
penicillin-binding protein	-	Staphylococcus aureus
penicillin-binding protein	-	Haemophilus influenzae
penicillin-binding protein	-	Bacillus subtilis
penicillin-binding protein	-	Escherichia coli
penicillin-binding protein	-	Neisseria gonorrhoeae
penicillin-binding protein	-	Streptococcus pneumoniae
penicillin-binding protein	-	Streptomyces sp.
penicillin-binding protein	-	Caulobacter vibrioides
penicillin-binding protein	-	Streptomyces sp. R61
penicillin-binding protein	-	Streptomyces sp. K15
transpeptidase	-	Staphylococcus aureus
transpeptidase	-	Haemophilus influenzae
transpeptidase	-	Bacillus subtilis
transpeptidase	-	Escherichia coli
transpeptidase	-	Neisseria gonorrhoeae
transpeptidase	-	Streptococcus pneumoniae
transpeptidase	-	Streptomyces sp.
transpeptidase	-	Caulobacter vibrioides
transpeptidase	-	Streptomyces sp. R61
transpeptidase	-	Streptomyces sp. K15