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Literature summary 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
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.21.62 | industry | the enzyme shows excellent performance in stain removal from cotton fabric and good compatibility with several commercial laundry detergent formulations, suggesting that it has high potential for use in various industrial applications | Fusarium equiseti |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.21.62 | gene prtS8A, DNA and amino acid sequence determination and analysis, fusion to the Trichoderma reesei cbh1 (cel7A) promoter and recombinant expression in Trichoderma reesei | Fusarium equiseti |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.21.62 | additional information | - |
additional information | Michaelis-Menten kinetics using Lineweaver-Burk and Hanes plots at pH 8.5 and 22°C, purified recombinant enzyme | Fusarium equiseti |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.62 | extracellular | - |
Fusarium equiseti | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.62 | Ca2+ | required, the presence of a low-affinity Ca2+ binding site formed by the backbone carbonyls cannot be excluded based on the amino acid sequence comparisons | Fusarium equiseti |  |
| 3.4.21.62 | Mg2+ | required | Fusarium equiseti | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.62 | 29000 | - |
x * 29000, native enzyme, SDS-PAGE, x * 29141, sequence calculation, x * 29140, recombinant enzyme, mass spectrometry | Fusarium equiseti |
| 3.4.21.62 | 29140 | - |
x * 29000, native enzyme, SDS-PAGE, x * 29141, sequence calculation, x * 29140, recombinant enzyme, mass spectrometry | Fusarium equiseti |
| 3.4.21.62 | 29141 | - |
x * 29000, native enzyme, SDS-PAGE, x * 29141, sequence calculation, x * 29140, recombinant enzyme, mass spectrometry | Fusarium equiseti |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.62 | Fusarium equiseti | - |
gene prtS8A | - |
| 3.4.21.62 | Fusarium equiseti CBS119568 | - |
gene prtS8A | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.21.62 | proteolytic modification | sites of primary autoproteolysis of the purified recombinant Fe protease are Leu2-Thr3, Gly11-Leu12, Trp143-Ala144, Ala173-Ser174, Ala179-Asn180, and Trp219-Tyr220 (numbered according to the amino acids in the mature protease) | Fusarium equiseti |
| 3.4.21.62 | proteolytic modification | sites of primary autoproteolysis of the purified recombinant Fe protease areLeu2-Thr3, Gly11-Leu12, Trp143-Ala144, Ala173-Ser174, Ala179-Asn180, and Trp219-Tyr220 (numbered according to the amino acids in the mature protease) | Fusarium equiseti |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.21.62 | native extracellular enzyme from culture supernatant by anion exchangc chromatography, ammonium sulfate fractionation, hydrophobic interaction chromatography, ultrafiltration, and gel filtration, recombinant enzyme from Trichoderma reesei | Fusarium equiseti |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.62 | beta-casein + H2O | from bovine milk | Fusarium equiseti | ? | - |
? | |
| 3.4.21.62 | beta-casein + H2O | from bovine milk | Fusarium equiseti CBS119568 | ? | - |
? | |
| 3.4.21.62 | Cytochrome c + H2O | from equine heart | Fusarium equiseti | ? | - |
? | |
| 3.4.21.62 | Cytochrome c + H2O | from equine heart | Fusarium equiseti CBS119568 | ? | - |
? | |
| 3.4.21.62 | additional information | the Fusarium equiseti Fe protease has a broad substrate specificity, almost all amino acid residues are accepted at position P1, even though it shows some preference for cleavage at the C-terminal side of asparagine and histidine residues. The S4 subsite of Fe protease favors aspartic acid and threonine, substrate specificity and comprison to other subtilisin and selected fungal subtilisin-like proteases, overview | Fusarium equiseti | ? | - |
? | |
| 3.4.21.62 | additional information | the Fusarium equiseti Fe protease has a broad substrate specificity, almost all amino acid residues are accepted at position P1, even though it shows some preference for cleavage at the C-terminal side of asparagine and histidine residues. The S4 subsite of Fe protease favors aspartic acid and threonine, substrate specificity and comprison to other subtilisin and selected fungal subtilisin-like proteases, overview | Fusarium equiseti CBS119568 | ? | - |
? | |
| 3.4.21.62 | Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O | - |
Fusarium equiseti | Suc-Ala-Ala-Pro-Phe + 4-nitroaniline | - |
? | |
| 3.4.21.62 | Suc-Ala-Ala-Pro-Phe-4-nitroanilide + H2O | - |
Fusarium equiseti CBS119568 | Suc-Ala-Ala-Pro-Phe + 4-nitroaniline | - |
? | |
| 3.4.21.62 | ubiquitin + H2O | from bovine blood cells | Fusarium equiseti | ? | - |
? | |
| 3.4.21.62 | ubiquitin + H2O | from bovine blood cells | Fusarium equiseti CBS119568 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.62 | ? | x * 29000, native enzyme, SDS-PAGE, x * 29141, sequence calculation, x * 29140, recombinant enzyme, mass spectrometry | Fusarium equiseti |
| 3.4.21.62 | More | N-terminal and internal amino acid sequencing, overview | Fusarium equiseti |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.62 | Fe protease | - |
Fusarium equiseti |
| 3.4.21.62 | subtilisin-like protease | - |
Fusarium equiseti |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.62 | 60 | - |
recombinant enzyme | Fusarium equiseti |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.62 | 30 | 70 | 40% of maximal activity at 30°C and 70°C, 70% at 50°C, at pH 8.6, profile overview | Fusarium equiseti |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.62 | 10 | - |
with beta-casein | Fusarium equiseti |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.62 | 6 | 10 | over 60% of maximum activity at pH 6-10, with a sharp decline in activity above pH 10, at 50°C, profile overview | Fusarium equiseti |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.21.62 | evolution | the subtilisin-like proteases share the same catalytic mechanism as the trypsin-like proteases, depending upon the hydroxyl group of a serine residue. The catalytic triad of subtilisin-like proteases is composed of Asp, His, and Ser. Due to its different specificity compared to the members of the S8 family of clan SB of proteases, the Fe protease might be a protease distinct from previously defined IUBMB groups of proteases, it is no member of the the S8 peptidase family | Fusarium equiseti |
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