Any feedback?
Literature summary for 3.4.24.26 extracted from
- Pseudomonas aeruginosa A2 elastase: Purification, characterization and biotechnological applications (2012), Int. J. Biol. Macromol., 50, 679-686.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the pro-sequence, consisting of 174 amino acids, is cleaved by autoproteolytic processing in the periplasm to produce the active, mature elastase of 301 amino acids | Pseudomonas aeruginosa |
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | A2 protease is usable for shrimp waste deproteinization in the process of chitin preparation, percent of protein removal after 3 h hydrolysis at 40°C with an enzyme/substrate ratio of 5 U/mg protein is about 75%. A2 proteolytic preparation also demonstrates powerful depilating capabilities of hair removal from bovine skin | Pseudomonas aeruginosa |
| industry | A2 protease is usable for shrimp waste deproteinization in the process of chitin preparation, percent of protein removal after 3 h hydrolysis at 40°C with an enzyme/substrate ratio of 5 U/mg protein is about 75%. A2 proteolytic preparation also demonstrates powerful depilating capabilities of hair removal from bovine skin | Pseudomonas aeruginosa |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene lasB, DNA and amino acid sequence determination and analysis | Pseudomonas aeruginosa |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | 18.8% inhibition at 5 mM | Pseudomonas aeruginosa |  |
| Ca2+ | 10.6% inhibition at 5 mM | Pseudomonas aeruginosa | |
| Cu2+ | complete inhibition at 5 mM | Pseudomonas aeruginosa | |
| EDTA | 57.7% inhibition at 2 mM, 68.5% inhibition at 5 mM | Pseudomonas aeruginosa | |
| Hg2+ | complete inhibition at 5 mM | Pseudomonas aeruginosa | |
| Mg2+ | 16.4% inhibition at 5 mM | Pseudomonas aeruginosa | |
| Mn2+ | 81.9% inhibition at 5 mM | Pseudomonas aeruginosa | |
| additional information | no inhibition by dithio-bis(nitrobenzoic acid) and phenylmethylsulfonyl fluoride, and by K+ and Na+ | Pseudomonas aeruginosa | |
| Zn2+ | complete inhibition at 5 mM | Pseudomonas aeruginosa | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme is secreted | Pseudomonas aeruginosa | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | metalloprotease, the enzynme contains the typical metalloendopeptidases consensus zinc-binding sequence HEXXH | Pseudomonas aeruginosa |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 33030 | - |
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation | Pseudomonas aeruginosa |
| 34000 | - |
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation | Pseudomonas aeruginosa |
| 53610 | - |
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation | Pseudomonas aeruginosa |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| additional information | the enzyme is stable in the presence of organic solvents mainly diethyl ether and DMSO | Pseudomonas aeruginosa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | - |
isolated from marine water in Sfax city, Tunisia, gene lasB | - |
| Pseudomonas aeruginosa A2 | - |
isolated from marine water in Sfax city, Tunisia, gene lasB | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the pro-sequence, consisting of 174 amino acids, is cleaved by autoproteolytic processing in the periplasm to produce the active, mature elastase of 301 amino acids | Pseudomonas aeruginosa |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme 2.23fold to homogeneity by ultrafiltration, gel filtration, and anion exchange chromatography | Pseudomonas aeruginosa |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 81100 | - |
purified enzyme, pH 8.0, 37°C | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein + H2O | - |
Pseudomonas aeruginosa | ? | - |
? | |
| casein + H2O | - |
Pseudomonas aeruginosa A2 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation | Pseudomonas aeruginosa |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| A2 elastase | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Pseudomonas aeruginosa |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 80 | activity range, profile overview | Pseudomonas aeruginosa |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | purified enzyme, completely stable at 30°C and 40°C after 60 min, A2 protease retains about 80% and 60% of its initial activity after incubation for 60 min at 50°C and 60°C, respectively | Pseudomonas aeruginosa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
- |
Pseudomonas aeruginosa |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 10 | activity range, profile overview | Pseudomonas aeruginosa |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 11 | purified enzyme, 60 min, loss of 30% activity at pH 5.0 and of 50% at pH 11.0, completely stable at pH 6.0-10.0, profile overview | Pseudomonas aeruginosa |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Pseudomonas aeruginosa | sequence calculation | - |
5.88 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the typical metalloendopeptidases consensus zinc-binding sequence HEXXH and the catalytic residues in the active site are conserved in the A2 elastase | Pseudomonas aeruginosa |
| additional information | the N-terminal signal peptide consists of 23 residues bordered with the signal peptidase recognition site Ala-Phe-Ala-Ala | Pseudomonas aeruginosa |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
