Literature summary extracted from
Zhang, L.; Conway, J.F.; Thibodeau, P.H.
Calcium-induced folding and stabilization of the Pseudomonas aeruginosa alkaline protease (2012), J. Biol. Chem., 287, 4311-4322.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.4.24.40 |
expression of wild-type and mutant AP proteins and domains at high levels in inclusion bodies |
Pseudomonas aeruginosa |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.4.24.40 |
additional information |
generation of a series of full-length and truncation mutants for structural and functional studies, overview. DELTAN-AP shows increased thermal sensitivity compared with the wild-type enzyme. At 42°C, protease activity decreases by 50%, and at 55°C, protease activity decreases by 90% when compared with the full-length AP in 2 mM Ca2+ |
Pseudomonas aeruginosa |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.4.24.40 |
Ca2+ |
calcium-regulated alkaline protease, role of Ca2+ in enzyme folding and activation: Ca2+binding induces RTX folding, which serves to chaperone the folding of the protease domain. Subsequent association of the RTX domain with an N-terminal alpha-helix stabilizes AP, Ca2+ regulates the RTX family of virulence factors, overview |
Pseudomonas aeruginosa |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.24.40 |
Pseudomonas aeruginosa |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.4.24.40 |
recombinant refolded His-tagged wild-type and mutant AP proteins and domains from inclusion bodies by nickel affinity chromatography |
Pseudomonas aeruginosa |
Renatured (Commentary)
EC Number |
Renatured (Comment) |
Organism |
---|
3.4.24.40 |
recombinant His-tagged wild-type and mutant AP proteins and domains under denaturing conditions are refolded from inclusion bodies using either urea for RTX, or guanidine HCl for full-length and truncation mutants |
Pseudomonas aeruginosa |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.24.40 |
casein + H2O |
- |
Pseudomonas aeruginosa |
? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.24.40 |
calcium-regulated alkaline protease |
- |
Pseudomonas aeruginosa |
3.4.24.40 |
Pseudomonas aeruginosa alkaline protease |
- |
Pseudomonas aeruginosa |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
3.4.24.40 |
additional information |
- |
comparison of full-length and truncation mutants, DELTAN-AP shows increased thermal sensitivity compared with the wild-type enzyme. At 42°C, protease activity decreases by 50%, and at 55°C, protease activity decreases by 90% when compared with the full-length AP in 2 mM Ca2+ |
Pseudomonas aeruginosa |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.4.24.40 |
evolution |
the calcium-regulated alkaline protease is a member of the repeats in toxin, RTX, family of proteins |
Pseudomonas aeruginosa |
3.4.24.40 |
physiological function |
the calcium-regulated alkaline protease is implicated in multiple modes of infection |
Pseudomonas aeruginosa |