Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.24.26 extracted from

  • Bian, F.; Yue, S.; Peng, Z.; Zhang, X.; Chen, G.; Yu, J.; Xuan, N.; Bi, Y.
    A comprehensive alanine-scanning mutagenesis study reveals roles for salt bridges in the structure and activity of Pseudomonas aeruginosa elastase (2015), PLoS ONE, 10, e121108.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
D168A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa
D189A site-directed mutagenesis, the mutant shows decreased thermal stabilities and increased activities compared to the wild-type enzyme Pseudomonas aeruginosa
D201A site-directed mutagenesis, the mutant shows slightly increased thermal stability and slightly decreased activity compared to the wild-type enzyme Pseudomonas aeruginosa
E249A site-directed mutagenesis, the mutant shows both decreased thermal stability and decreased activity compared to the wild-type enzyme Pseudomonas aeruginosa
R179A site-directed mutagenesis, the mutant shows decreased thermal stabilities and increased activities compared to the wild-type enzyme Pseudomonas aeruginosa
R198A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa
R205A site-directed mutagenesis, the mutant shows slightly increased thermal stability and slightly decreased activity compared to the wild-type enzyme Pseudomonas aeruginosa
R245A site-directed mutagenesis Pseudomonas aeruginosa
R253A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa
R279A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by ammonium sulfate fractionation, anion exchange chromatography Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-(2-furylacryloyl)glycyl-L-leucine amide + H2O
-
Pseudomonas aeruginosa ?
-
?
casein + H2O
-
Pseudomonas aeruginosa ?
-
?

Synonyms

Synonyms Comment Organism
elastase
-
Pseudomonas aeruginosa
PAE
-
Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Pseudomonas aeruginosa

General Information

General Information Comment Organism
evolution the enzyme is an M4 family metalloprotease Pseudomonas aeruginosa
additional information salt bidges in the enzyme, structure overview. Relationship between salt bridges and stability/enzymatic activity, structure analysis and molecular dynamics using crystal structure with PDB ID 1EZM, overview Pseudomonas aeruginosa