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Information on EC 3.4.17.13 - Muramoyltetrapeptide carboxypeptidase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HTZ1

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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9HTZ1 not found.
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl-/-D-alanine
Synonyms
ld-carboxypeptidase, carboxypeptidase ii, ldca1, l,d-carboxypeptidase a, l-lysyl-d-alanine carboxypeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LD-Carboxypeptidase
-
Carboxypeptidase II
-
-
-
-
Carboxypeptidase IIW
-
-
-
-
Carboxypeptidase, lysyl-D-alanine
-
-
-
-
Carboxypeptidase, muramoyltetrapeptide
-
-
-
-
L-Lysyl-D-alanine carboxypeptidase
-
-
-
-
LD-Carboxypeptidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl-/-D-alanine
show the reaction diagram
the enzyme is a serine peptidase with a Ser115-His285-Glu217 catalytic triad
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
CAS REGISTRY NUMBER
COMMENTARY hide
60063-80-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GlcNAc-MurNAc tetrapeptide + H2O
?
show the reaction diagram
substrate prepared from purified murein by lysozyme, cleaves specifically between meso-diaminopimelic acid and D-alanine
-
-
?
peptidoglycan + H2O
?
show the reaction diagram
the enzyme is involved in peptidoglycan recycling
-
-
?
additional information
?
-
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
peptidoglycan + H2O
?
show the reaction diagram
the enzyme is involved in peptidoglycan recycling
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34600
2 * 34600, about, sequence calculation
51000
recombinant enzyme, high salt condition gel filtration
56000
recombinant enzyme, low salt condition gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 34600, about, sequence calculation
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type enzyme and mutants S115A and H285A, sitting drop vapour diffusion method, 0.004 ml of 6 mg/ml protein containing solution is mixed with an equal volume of reservoir solution containing 20 mM CaCl2 dihydrate, 0.1 M sodium acetate trihydrate, pH 4.6, and 30% v/v 2-methyl-2,4-pentanediol, room temperature, 6 mg/ml selenomethionine-labeled enzyme from 50 mM citric acid, pH 4.5, 21°C, X-ray diffraction structure determination and analysis at 1.5-2.4 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E217A
site-directed mutagenesis, nearly inactive mutant, lack of activity might possibly be due to a folding defect, no crystallization of the mutant enzyme
H285A
site-directed mutagenesis, nearly inactive mutant, lack of activity is not due to a folding defect
S115A
site-directed mutagenesis, nearly inactive mutant, lack of activity is not due to a folding defect
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Korza, H.J.; Bochtler, M.
Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow
J. Biol. Chem.
280
40802-40812
2005
Pseudomonas aeruginosa (Q9HTZ1), Pseudomonas aeruginosa
Manually annotated by BRENDA team