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Information on EC 3.4.16.4 - serine-type D-Ala-D-Ala carboxypeptidase and Organism(s) Bacillus subtilis and UniProt Accession P39844

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Bacillus subtilis
UNIPROT: P39844 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
Synonyms
transpeptidase, penicillin-binding protein, pbp2x, pbp1a, pbp1b, penicillin binding proteins, pbp 2, pbp 3, pbp 5, dd-peptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
penicillin-binding protein 4a
-
carboxypeptidase I
-
-
-
-
CPase
-
-
-
-
D-alanine carboxypeptidase
-
-
-
-
D-alanine carboxypeptidase I
-
-
-
-
D-alanyl carboxypeptidase
-
-
-
-
D-alanyl-D-alanine carboxypeptidase
-
-
-
-
D-Alanyl-D-alanine hydrolase
-
-
-
-
D-alanyl-D-alanine peptidase
-
-
-
-
D-alanyl-D-alanine transpeptidase
-
-
D-alanyl-D-alanine-carboxypeptidase
-
-
-
-
D-alanyl-D-alanine-cleaving peptidase
-
-
-
-
D-alanyl-D-alanine-cleaving-peptidase
-
-
-
-
DD-Carboxypeptidase
DD-peptidase
DD-transpeptidase
-
-
-
-
PBP-5*
-
-
-
-
PBP-6B
-
-
-
-
penicillin binding protein 5
-
-
-
-
penicillin-binding protein
-
-
transpeptidase
-
-
VanX
-
-
-
-
VanY
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
CAS REGISTRY NUMBER
COMMENTARY hide
9077-67-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Nalpha-acetyl-L-Lys-D-Ala-D-Ala + H2O
?
show the reaction diagram
substrate is used to detect the hydrolyzing activity of PBP4a
-
-
?
bocillin FL
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine + H2O
UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanine + D-alanine
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-muramyl-L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine
?
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
penicillin
-
binds covalently to Ser36, Bacillus subtilis, Bacillus stearothermophilus
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
GFP-PBP5 localizes to the septum and in concentrated spots along the lateral wall
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the protein alone is solved at a resolution of 2.1 A, and in complex with D-alpha-aminopymelyl-eta-D-alanyl-D-alanine at a resolution of 2.8 A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using a Heparin-Sepharose CL-6B column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coliDH5alpha
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
bacterial DD-peptidases are still an enticing target for antibacterial agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yocum, R.R.; Waxman, D.J.; Rasmussen, J.R.; Strominger, J.L.
Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases
Proc. Natl. Acad. Sci. USA
76
2730-2734
1979
Geobacillus stearothermophilus, Bacillus subtilis
Manually annotated by BRENDA team
Scheffers, D.J.; Jones, L.J.F.; Errington, J.
Several distinct localization patterns for penicillin-binding proteins in Bacillus subtilis
Mol. Microbiol.
51
749-764
2004
Bacillus subtilis
Manually annotated by BRENDA team
Pratt, R.F.
Substrate specificity of bacterial DD-peptidases (penicillin-binding proteins)
Cell. Mol. Life Sci.
65
2138-2155
2008
Bacillus subtilis, Caulobacter vibrioides, Streptomyces sp., Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Staphylococcus aureus, Neisseria gonorrhoeae, Streptomyces sp. R61, Streptomyces sp. K15
Manually annotated by BRENDA team
Sauvage, E.; Duez, C.; Herman, R.; Kerff, F.; Petrella, S.; Anderson, J.W.; Adediran, S.A.; Pratt, R.F.; Frere, J.M.; Charlier, P.
Crystal structure of the Bacillus subtilis penicillin-binding protein 4a, and its complex with a peptidoglycan mimetic peptide
J. Mol. Biol.
371
528-539
2007
Bacillus subtilis (P39844)
Manually annotated by BRENDA team