Literature summary for 3.4.17.13 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.

Search for more literature for 3.4.17.13

Cloned(Commentary)

Cloned (Comment)	Organism
DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli	Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants	Comment	Organism
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
H285A	site-directed mutagenesis, nearly inactive mutant, lack of activity is not due to a folding defect	Pseudomonas aeruginosa
S115A	site-directed mutagenesis, nearly inactive mutant, lack of activity is not due to a folding defect	Pseudomonas aeruginosa

Inhibitors

Inhibitors	Comment	Organism	Structure
nocardicin A	-	Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
34600	-	2 * 34600, about, sequence calculation	Pseudomonas aeruginosa
51000	-	recombinant enzyme, high salt condition gel filtration	Pseudomonas aeruginosa
56000	-	recombinant enzyme, low salt condition gel filtration	Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
peptidoglycan + H2O	Pseudomonas aeruginosa	the enzyme is involved in peptidoglycan recycling	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	Q9HTZ1	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli	Pseudomonas aeruginosa

Reaction

Reaction	Comment	Organism	Reaction ID
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	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
GlcNAc-MurNAc tetrapeptide + H2O	substrate prepared from purified murein by lysozyme, cleaves specifically between meso-diaminopimelic acid and D-alanine	Pseudomonas aeruginosa	?	-	?
additional information	the enzyme is a serine peptidase which cleaves between the L- and D-amino acids of bacterial peptidoglycan	Pseudomonas aeruginosa	?	-	?
peptidoglycan + H2O	the enzyme is involved in peptidoglycan recycling	Pseudomonas aeruginosa	?	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 34600, about, sequence calculation	Pseudomonas aeruginosa
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

Synonyms	Comment	Organism
LD-Carboxypeptidase	-	Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Pseudomonas aeruginosa

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	total turnover of wild-type and mutant enzymes in comparison	Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Pseudomonas aeruginosa