Literature summary extracted from
Korza, H.J.; Bochtler, M.
Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow (2005), J. Biol. Chem., 280, 40802-40812.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.4.17.13 |
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli |
Pseudomonas aeruginosa |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.4.17.13 |
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 |
Pseudomonas aeruginosa |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.4.17.13 |
E217A |
site-directed mutagenesis, nearly inactive mutant, lack of activity might possibly be due to a folding defect, no crystallization of the mutant enzyme |
Pseudomonas aeruginosa |
3.4.17.13 |
H285A |
site-directed mutagenesis, nearly inactive mutant, lack of activity is not due to a folding defect |
Pseudomonas aeruginosa |
3.4.17.13 |
S115A |
site-directed mutagenesis, nearly inactive mutant, lack of activity is not due to a folding defect |
Pseudomonas aeruginosa |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.4.17.13 |
nocardicin A |
- |
Pseudomonas aeruginosa |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
3.4.17.13 |
34600 |
- |
2 * 34600, about, sequence calculation |
Pseudomonas aeruginosa |
3.4.17.13 |
51000 |
- |
recombinant enzyme, high salt condition gel filtration |
Pseudomonas aeruginosa |
3.4.17.13 |
56000 |
- |
recombinant enzyme, low salt condition gel filtration |
Pseudomonas aeruginosa |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
3.4.17.13 |
peptidoglycan + H2O |
Pseudomonas aeruginosa |
the enzyme is involved in peptidoglycan recycling |
? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.17.13 |
Pseudomonas aeruginosa |
Q9HTZ1 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.4.17.13 |
recombinant enzyme from Escherichia coli |
Pseudomonas aeruginosa |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
3.4.17.13 |
hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl-/-D-alanine |
the enzyme is a serine peptidase with a Ser115-His285-Glu217 catalytic triad |
Pseudomonas aeruginosa |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.17.13 |
GlcNAc-MurNAc tetrapeptide + H2O |
substrate prepared from purified murein by lysozyme, cleaves specifically between meso-diaminopimelic acid and D-alanine |
Pseudomonas aeruginosa |
? |
- |
? |
|
3.4.17.13 |
additional information |
the enzyme is a serine peptidase which cleaves between the L- and D-amino acids of bacterial peptidoglycan |
Pseudomonas aeruginosa |
? |
- |
? |
|
3.4.17.13 |
peptidoglycan + H2O |
the enzyme is involved in peptidoglycan recycling |
Pseudomonas aeruginosa |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.4.17.13 |
dimer |
2 * 34600, about, sequence calculation |
Pseudomonas aeruginosa |
3.4.17.13 |
More |
the enzyme consists of an N-terminal beta-sheet and a C-terminal beta-barrel domain, at the interface of the two domains Ser115 adopts a highly strained conformation in a strand-turn-helix motif similar to the nucleophilic elbow in alphabeta-hydrolases, domain structure, overview |
Pseudomonas aeruginosa |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.17.13 |
LD-Carboxypeptidase |
- |
Pseudomonas aeruginosa |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
3.4.17.13 |
37 |
- |
assay at |
Pseudomonas aeruginosa |
Turnover Number [1/s]
EC Number |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Comment |
Organism |
Structure |
---|
3.4.17.13 |
additional information |
- |
additional information |
total turnover of wild-type and mutant enzymes in comparison |
Pseudomonas aeruginosa |
|
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.4.17.13 |
7 |
- |
assay at |
Pseudomonas aeruginosa |