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Literature summary extracted from
- Glutamyl endopeptidases: structure, function, and practical application (2003), Russ. J. Bioorg. Chem., 29, 511-522.
No PubMed abstract available
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.21.19 | analysis | study of structure-function organization of anti-HIV and antitumor proteins MAP30 and GAP31 by limited proteolysis with V8-GSE, enzym may be useful for studying other proteins as well | Staphylococcus aureus |
| 3.4.21.19 | synthesis | enzyme can be used as catalyst for peptide synthesis in hydrophilic organic solvents with low water content, e.g. acetonitrile, overview | Staphylococcus aureus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.21.19 | enzyme is crystallized complexed with substrate Boc-Ala-Ala-Pro-Glu-4-nitroanilide, X-ray structure determination and analysis at 2.0 A resolution | Streptomyces griseus |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.19 | additional information | enzyme is a metalloprotease | Bacillus subtilis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.19 | Bacillus licheniformis | - |
- |
- |
| 3.4.21.19 | Bacillus subtilis | - |
enzyme possesses Cys at position 193 instead of highly conserved Gly, the most conserved residue of the trypsin enzyme family | - |
| 3.4.21.19 | Staphylococcus aureus | - |
- |
- |
| 3.4.21.19 | Staphylococcus aureus V8 | - |
- |
- |
| 3.4.21.19 | Streptomyces griseus | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- | catalytic tetrad of His213, Asp102, Ser195, and Trp214, computer modeling of S1 and S'1 sites of the enzyme's active site | Staphylococcus aureus | |
| 3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- | catalytic triad of His, Asp, and Ser | Bacillus subtilis | |
| 3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- | catalytic triad of His, Asp, and Ser, computer modeling of active site structure, S1-substrate binding site, and substrate binding mechanism | Bacillus licheniformis | |
| 3.4.21.19 | Preferential cleavage: Glu-/-, Asp-/- | catalytic triad of His, Asp, and Ser, substrate binding mechanism and structure | Streptomyces griseus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.19 | benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Staphylococcus aureus | ? | - |
? |  |
| 3.4.21.19 | benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Bacillus licheniformis | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Staphylococcus aureus V8 | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Staphylococcus aureus | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Bacillus licheniformis | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Staphylococcus aureus V8 | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Staphylococcus aureus | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Bacillus licheniformis | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala carboxyethylthioester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Staphylococcus aureus | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala carboxyethylthioester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Bacillus licheniformis | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala carboxyethylthioester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Staphylococcus aureus V8 | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala carboxymethylthioester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Staphylococcus aureus | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala carboxymethylthioester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Bacillus licheniformis | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala carboxymethylthioester + H2O | enzyme also performs acyl-transfer reaction with substrate mimetics | Staphylococcus aureus V8 | ? | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala-Ala-Glu-methyl ester + leucine * HCl | peptide synthesis | Staphylococcus aureus | benzyloxycarbonyl-Ala-Ala-Glu-Leu + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Ala-Glu-methyl ester + leucine * HCl | peptide synthesis | Staphylococcus aureus | benzyloxycarbonyl-Ala-Glu-Leu + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Asp-methyl ester + Ala-Ala-D-hydroxyalanine | peptide synthesis, low activity at 25°C, but high activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Asp-Ala-Ala-D-hydroxyalanine + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Asp-methyl ester + Ala-Ala-hydroxyproline | peptide synthesis, lower activity at 25°C, but high activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Asp-Ala-Ala-hydroxyproline + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Asp-methyl ester + Ala-D-hydroxyalanine | peptide synthesis, very low activity at 25°C, but moderate activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Asp-Ala-D-hydroxyalanine + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Asp-methyl ester + Ala-hydroxyaspartate | peptide synthesis, low activity at 25°C, but high activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Asp-Ala-hydroxyaspartate + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Asp-methyl ester + Ala-hydroxyglutamate | peptide synthesis, very low activity at 25°C, but high activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Asp-Ala-hydroxyglutamate + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Asp-methyl ester + Ala-hydroxyproline | peptide synthesis, no activity at 25°C, only low activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Asp-Ala-hydroxyproline + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Asp-methyl ester + Asp-Gly | peptide synthesis, no activity at 25°C, but moderate activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Asp-Asp-Gly + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Asp-methyl ester + aspartate | peptide synthesis, no activity at 25°C, but high activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Asp-Asp + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Asp-methyl ester + Glu-Gly | peptide synthesis, no activity at 25°C, but moderate activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Asp-Glu-Gly + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Asp-methyl ester + glutamate | peptide synthesis, no activity at 25°C, but high activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Asp-Glu + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + Ala-Ala-D-Ala | peptide synthesis, low activity at 25°C, but high activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Glu-Ala-Ala-D-Ala + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + Ala-Ala-Pro | peptide synthesis, lower activity at 25°C, but high activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Glu-Ala-Ala-Pro + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + Ala-Asp | peptide synthesis, no activity at 25°C, but high activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Glu-Ala-Asp + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + Ala-D-Ala | peptide synthesis, no activity at 25°C, but moderate activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Glu-Ala-D-Ala + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + Ala-Glu | peptide synthesis, no activity at 25°C, but high activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Glu-Ala-Glu + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + Ala-Pro | peptide synthesis, no activity at 25°C, only low activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Glu-Ala-Pro + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + Asp-Gly | peptide synthesis, no activity at 25°C, but moderate activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Glu-Asp-Gly + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + Glu-Gly | peptide synthesis, no activity at 25°C, but low activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Glu-Glu-Gly + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + L-aspartate | peptide synthesis, no activity at 25°C, but moderate activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Glu-Asp + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + L-glutamate | peptide synthesis, no activity at 25°C, but moderate activity at -15°C | Bacillus licheniformis | benzyloxycarbonyl-Glu-Glu + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + L-tryptophan | peptide synthesis | Staphylococcus aureus | benzyloxycarbonyl-Glu-Trp + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + Leu-Gly | peptide synthesis | Staphylococcus aureus | benzyloxycarbonyl-Glu-Leu-Gly + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + leucine | peptide synthesis | Staphylococcus aureus | benzyloxycarbonyl-Glu-Leu + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Glu-methyl ester + Phe-Gly | peptide synthesis | Staphylococcus aureus | benzyloxycarbonyl-Glu-Phe-Gly + methanol | - |
? | |
| 3.4.21.19 | benzyloxycarbonyl-Pro-Leu-Gly-S-CH2-COOH + LAFARAEAFG | acylation of peptide fragment by substrate mimetic | Staphylococcus aureus | benzyloxycarbonyl-PLGLAFARAEAFG + HS-CH2-COOH | product formation 55% | ? | |
| 3.4.21.19 | benzyloxycarbonyl-S-CH2-COOH + LAFARAEAF-hydroxyglycine | acylation of peptide fragment by substrate mimetic | Staphylococcus aureus | benzyloxycarbonyl-LAFARAEAF-hydroxyglycine + HS-CH2-COOH | product formation 99% | ? | |
| 3.4.21.19 | beta-type parvalbumin + H2O | from the frog Rana catesbeiana | Staphylococcus aureus | peptide fragments | mass spectrometry for identification | ? | |
| 3.4.21.19 | bovine hemoglobin + H2O | in presence of SDS | Staphylococcus aureus | peptide fragments | peptide mapping, 2 peptide fragments are Leu76-Pro-Gly-Ala-Leu-Ser-Glu82 and Lys94-Leu-His-Val-Asp-Pro-Glu100 | ? | |
| 3.4.21.19 | hemocyanin + H2O | hydrolysis of 2 isozymes of hemocyanin KLH1 and KLH2 from shellfish Megatura crenulata at Glu-Xaa and Asp-Xaa bonds | Staphylococcus aureus | peptide fragments | - |
? | |
| 3.4.21.19 | additional information | no peptide synthesis activity with proline and D-leucine, active in semienzymatic synthesis of human growth hormone | Bacillus licheniformis | ? | - |
? | |
| 3.4.21.19 | additional information | substrate specificity is pH-dependent due to active site His213, peptide synthesizing substrate specificity, no peptide synthesizing activity with benzyloxycarbonyl-Asp-methyl ester | Staphylococcus aureus | ? | - |
? | |
| 3.4.21.19 | additional information | substrate specificity is pH-dependent due to active site His213, peptide synthesizing substrate specificity, no peptide synthesizing activity with benzyloxycarbonyl-Asp-methyl ester | Staphylococcus aureus V8 | ? | - |
? | |
| 3.4.21.19 | tert-butyloxycarbonyl-Ala-Ala-Pro-Glu-4-nitroanilide + H2O | - |
Streptomyces griseus | tert-butyloxycarbonyl-Ala-Ala-Pro-Glu + 4-nitroaniline | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.19 | More | structural and functional organization, overview, enzyme shows 2 beta-barrels and a C-terminal alpha-helix when complexed with substrate Boc-Ala-Ala-Pro-Glu-4-nitroanilide | Streptomyces griseus |
| 3.4.21.19 | More | structural and functional rganization, overview | Staphylococcus aureus |
| 3.4.21.19 | More | structural and functional rganization, overview | Bacillus subtilis |
| 3.4.21.19 | More | structural and functional rganization, overview | Bacillus licheniformis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.19 | BL-GSE | - |
Bacillus licheniformis |
| 3.4.21.19 | BS-GSE | - |
Bacillus subtilis |
| 3.4.21.19 | glutamic acid-specific endopeptidase | - |
Staphylococcus aureus |
| 3.4.21.19 | glutamic acid-specific endopeptidase | - |
Bacillus subtilis |
| 3.4.21.19 | glutamic acid-specific endopeptidase | - |
Bacillus licheniformis |
| 3.4.21.19 | glutamic acid-specific endopeptidase | - |
Streptomyces griseus |
| 3.4.21.19 | SG-GSE | - |
Streptomyces griseus |
| 3.4.21.19 | V8 protease | - |
Staphylococcus aureus |
| 3.4.21.19 | V8-GSE | - |
Staphylococcus aureus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.19 | additional information | - |
peptide synthesis at -15°C | Bacillus licheniformis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.19 | 7.3 | 8 | - |
Bacillus licheniformis |
| 3.4.21.19 | 9 | - |
- |
Streptomyces griseus |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.4.21.19 | Staphylococcus aureus | 2 ionogenic groups | - |
additional information |
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