Any feedback?
Literature summary for 3.4.21.62 extracted from
- A new subtilase-like protease deriving from Fusarium equiseti with high potential for industrial applications (2015), Appl. Biochem. Biotechnol., 177, 407-430 .
Application
| Application | Comment | Organism |
|---|---|---|
| detergent | the Fe protease has an excellent stain removal effect especially on blood and egg stains | Fusarium equiseti |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Fe prtS8A, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of the enzyme under control of the Trichoderma reesei cbh1 (cel7A) promoter in Escherichia coli strain XL10-Gold, and functional recombinant expression in Trichoderma reesei protoplasts, the enzyme is secreted | Fusarium equiseti |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| H2O2 | the enzyme activity is reduced to 68% after a 20-min incubation with 0.33% hydrogen peroxide at 25°C in Tris buffer, substrate suc-Ala-Ala-Pro-Phe-4-nitroanilide, recombinant enzyme | Fusarium equiseti |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics using Lineweaver-Burk and Hanes plots | Fusarium equiseti | |
| 0.43 | - |
Suc-Ala-Ala-Pro-Phe-4-nitroanilide | recombinant enzyme, pH 8.5, 22°C | Fusarium equiseti | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Fusarium equiseti | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required, the enzyme sequence contains a low-affinity Ca2+ binding site | Fusarium equiseti | |
| Mg2+ | required | Fusarium equiseti | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Fusarium equiseti | - |
- |
- |
| Fusarium equiseti CBS 119568 | - |
- |
- |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| the enzyme activity is reduced to 68% after a 20-min incubation with 0.33% hydrogen peroxide at 25°C in Tris buffer, substrate suc-Ala-Ala-Pro-Phe-4-nitroanilide, recombinant enzyme | Fusarium equiseti |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | autoproteolytic degradation (autoproteolysis) of the purified recombinant Fe protease | Fusarium equiseti |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-casein + H2O | - |
Fusarium equiseti | ? | - |
? | |
| beta-casein + H2O | - |
Fusarium equiseti CBS 119568 | ? | - |
? | |
| additional information | the Fe protease is active against beta-casein, while it shows poor activity with cytochrome c and ubiquitin. beta-Casein is fully digested, while cytochrome c and ubiquitin are not. Autoproteolytic degradation (autoproteolysis) of the purified recombinant Fe protease. The Fe protease has a broad substrate specificity: almost all amino acid residues are accepted at positions P1-4 and P1'-P4'. The protease has a slight preference for His and Asn in position P1. There are only two amino acids, Pro and Asp, which are rarely found in position P1. Hydrophobic amino acids are overrepresented in position P2, but Gly, Asp, and the aromatic amino acids Phe and Tyr are rarely found in P2. Gly and Thr are favored in position P3 and Thr and Asp in position P4. Tyrosine is common in the P1' position, unlike Phe which is rarely found in position P1'. Compared to other proteases, the Fe protease has unique cleavage site specificity | Fusarium equiseti | ? | - |
? | |
| additional information | the Fe protease is active against beta-casein, while it shows poor activity with cytochrome c and ubiquitin. beta-Casein is fully digested, while cytochrome c and ubiquitin are not. Autoproteolytic degradation (autoproteolysis) of the purified recombinant Fe protease. The Fe protease has a broad substrate specificity: almost all amino acid residues are accepted at positions P1-4 and P1'-P4'. The protease has a slight preference for His and Asn in position P1. There are only two amino acids, Pro and Asp, which are rarely found in position P1. Hydrophobic amino acids are overrepresented in position P2, but Gly, Asp, and the aromatic amino acids Phe and Tyr are rarely found in P2. Gly and Thr are favored in position P3 and Thr and Asp in position P4. Tyrosine is common in the P1' position, unlike Phe which is rarely found in position P1'. Compared to other proteases, the Fe protease has unique cleavage site specificity | Fusarium equiseti CBS 119568 | ? | - |
? | |
| Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O | - |
Fusarium equiseti | Suc-Ala-Ala-Pro-Phe + 4-nitroaniline | - |
? | |
| Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O | - |
Fusarium equiseti CBS 119568 | Suc-Ala-Ala-Pro-Phe + 4-nitroaniline | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 29000, recombinant extracellular enzyme, SDS-PAGE, x * 29141, sequence calculation | Fusarium equiseti |
| More | enzyme N-terminal sequencing and mass spectrometric analysis | Fusarium equiseti |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Fe protease | - |
Fusarium equiseti |
| Fe prtS8A | - |
Fusarium equiseti |
| subtilase-like protease | - |
Fusarium equiseti |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Fusarium equiseti |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 70 | 70% of maximal activity at 50°C, maximal activity at 60°C, activity below 40% of maximal activity at 30°C, 40°C, and 70°C | Fusarium equiseti |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
purified recombinant enzyme, 60 min, 70% activity remaining | Fusarium equiseti |
| 40 | - |
purified recombinant enzyme, 60 min, 18% activity remaining | Fusarium equiseti |
| 50 | - |
purified recombinant enzyme, 60 min, 1% activity remaining | Fusarium equiseti |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 137 | - |
Suc-Ala-Ala-Pro-Phe-4-nitroanilide | recombinant enzyme, pH 8.5, 22°C | Fusarium equiseti | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 10 | - |
- |
Fusarium equiseti |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 11 | over 60% of maximum activity at range pH 6-10. The optimal pH for casein hydrolysis is pH 10, activity decreases strongly at pH 11 and a drastic loss of activity is observed at pH 12 | Fusarium equiseti |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Fusarium equiseti | sequence calculation | - |
9.3 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the S8 peptidase family | Fusarium equiseti |
| additional information | the Fe protease contains an insertion (amino acids 168-173 of the mature sequence) which is not present in the proteinase K sequence | Fusarium equiseti |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 318.6 | - |
Suc-Ala-Ala-Pro-Phe-4-nitroanilide | recombinant enzyme, pH 8.5, 22°C | Fusarium equiseti | |
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
