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Literature summary extracted from
- Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases (2008), Biol. Chem., 390, 277-285.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.21.19 | expressed in Escherichia coli | Staphylococcus aureus |
| 3.4.21.19 | expressed in Escherichia coli | Staphylococcus epidermidis |
| 3.4.21.19 | expressed in Escherichia coli | Staphylococcus warneri |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.21.19 | D189P | GluSE-P | Staphylococcus epidermidis |
| 3.4.21.19 | G176E/Q179E/Y185W/D189P/K191E/Y192F/S194G/S195A | GluV8DELTAC, the C-terminal 52 residues are deleted | Staphylococcus aureus |
| 3.4.21.19 | K191E/Y192F/S194G/S195A | GluSE-EFGA | Staphylococcus epidermidis |
| 3.4.21.19 | additional information | chimera A carries the N-terminal half of GluV8 (positions 1-118) and C-terminal half of GluSE (positions 119-216), chimera B carries GluV8, in which the third quarter from the N-terminus (positions 119-169) is replaced by the sequence of GluSE, chimera C carries GluV8, in which the C-terminal quarter (positions 170-216) is replaced by the sequence of GluSE, and Chimera D carries GluV8, in which the seventh part of 8 portions (positions 170-195) is replaced by the sequence of GluSE. The chimeric proteases as well as GluSE, GluV8, and GluV8DELTAC are converted to their mature forms by thermolysin treatment. When the 6 amino acids of GluSE are simultaneously replaced by those of GluV8, i.e., Y185W, D189P, L191E, Y192F, S194G, and S195A (designated GluSE-WPEFGA), the proteolytic activity of GluSE-WPEFGA becomes 3.8fold higher than that of GuV8DELTAC, in accordance with the super-activity of chimera B. GluSE/SW is composed of amino acids -66 to 169 of GluSE, which carried a putative proteolytic resistant region (residues 119-169) and amino acids 170-250 of GluSW. Activity of GluSE/SW becomes 4fold and 2fold higher than that of GluSE and GluSW | Staphylococcus epidermidis |
| 3.4.21.19 | additional information | chimera A carries the N-terminal half of GluV8 (positions 1-118) and C-terminal half of GluSE (positions 119-216), chimera B carries GluV8, in which the third quarter from the N-terminus (positions 119-169) is replaced by the sequence of GluSE, chimera C carries GluV8, in which the C-terminal quarter (positions 170-216) is replaced by the sequence of GluSE, and Chimera D carries GluV8, in which the seventh part of 8 portions (positions 170-195) is replaced by the sequence of GluSE. The chimeric proteases as well as GluSE, GluV8, and GluV8DELTAC are converted to their mature forms by thermolysin treatment. When the 6 amino acids of GluSE are simultaneously replaced by those of GluV8, i.e., Y185W, D189P, L191E, Y192F, S194G, and S195A (designated GluSE-WPEFGA), the proteolytic activity of GluSE-WPEFGA becomes 3.8fold higher than that of GuV8DELTAC, in accordance with the super-activity of chimera B | Staphylococcus aureus |
| 3.4.21.19 | additional information | GluSE/SW is composed of amino acids -66 to 169 of GluSE, which carried a putative proteolytic resistant region (residues 119-169) and amino acids 170-250 of GluSW. Activity of GluSE/SW becomes 4fold and 2fold higher than that of GluSE and GluSW | Staphylococcus warneri |
| 3.4.21.19 | Y185W | GluSE-W | Staphylococcus epidermidis |
| 3.4.21.19 | Y185W/D189P | the activity of GluSE with the two substitutions, i.e., Y185W and D189P (designated GluSE-WP), is equivalent to that of GluSE-WPEFGA | Staphylococcus epidermidis |
| 3.4.21.19 | Y185W/D189P/K191E/Y192F/S194G/S195A | GluSE/WPEFGA | Staphylococcus epidermidis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.21.19 | 0.3 | - |
Leu-Leu-Glu-4-methylcoumaryl-7-amide | chimera B | Staphylococcus epidermidis |  |
| 3.4.21.19 | 0.35 | - |
Leu-Leu-Glu-4-methylcoumaryl-7-amide | GluSE-WP | Staphylococcus epidermidis | |
| 3.4.21.19 | 1.32 | - |
Leu-Leu-Glu-4-methylcoumaryl-7-amide | GluSE-WAP | Staphylococcus epidermidis | |
| 3.4.21.19 | 2.84 | - |
Leu-Leu-Glu-4-methylcoumaryl-7-amide | GluSE-W | Staphylococcus epidermidis | |
| 3.4.21.19 | 4.15 | - |
Leu-Leu-Glu-4-methylcoumaryl-7-amide | GluSE-P | Staphylococcus epidermidis | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.19 | extracellular | - |
Staphylococcus epidermidis | - |
- |
| 3.4.21.19 | extracellular | - |
Staphylococcus warneri | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.19 | 28000 | - |
SDS-PAGE | Staphylococcus epidermidis |
| 3.4.21.19 | 32000 | - |
SDS-PAGE | Staphylococcus warneri |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.19 | Staphylococcus aureus | - |
- |
- |
| 3.4.21.19 | Staphylococcus epidermidis | - |
- |
- |
| 3.4.21.19 | Staphylococcus warneri | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.21.19 | - |
Staphylococcus aureus |
| 3.4.21.19 | - |
Staphylococcus epidermidis |
| 3.4.21.19 | - |
Staphylococcus warneri |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.19 | additional information | - |
the combination of W185, V188, and P189, which naturally occurr on GluV8, exerts the highest protease activity. Among them, W185 and P189 can not be replaced by other amino acids for the full activity, but V188 could be replaced by hydrophobic amino acids, such as L188 for the two substrates, F188 for AE-MCA and I188 for LLE-MCA | Staphylococcus aureus |
| 3.4.21.19 | additional information | - |
W185, A188, and A189 are responsible for the activity of GluSW | Staphylococcus warneri |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.19 | Ala-Glu-4-methylcoumaryl-7-amide + H2O | - |
Staphylococcus aureus | ? | - |
? | |
| 3.4.21.19 | Ala-Glu-4-methylcoumaryl-7-amide + H2O | - |
Staphylococcus epidermidis | ? | - |
? | |
| 3.4.21.19 | Ala-Glu-4-methylcoumaryl-7-amide + H2O | - |
Staphylococcus warneri | ? | - |
? | |
| 3.4.21.19 | Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O | - |
Staphylococcus aureus | ? | - |
? | |
| 3.4.21.19 | Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O | - |
Staphylococcus epidermidis | ? | - |
? | |
| 3.4.21.19 | Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O | - |
Staphylococcus warneri | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.19 | GluSE | - |
Staphylococcus epidermidis |
| 3.4.21.19 | GluSW | - |
Staphylococcus warneri |
| 3.4.21.19 | glutamyl endopeptidase | - |
Staphylococcus aureus |
| 3.4.21.19 | glutamyl endopeptidase | - |
Staphylococcus epidermidis |
| 3.4.21.19 | glutamyl endopeptidase | - |
Staphylococcus warneri |
| 3.4.21.19 | GluV8 | - |
Staphylococcus aureus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.21.19 | 6147 | - |
Leu-Leu-Glu-4-methylcoumaryl-7-amide | chimera B,W185, V188, P189 | Staphylococcus epidermidis | |
| 3.4.21.19 | 7681 | - |
Leu-Leu-Glu-4-methylcoumaryl-7-amide | GluSE-P, Y185, V188, P189 | Staphylococcus epidermidis | |
| 3.4.21.19 | 7695 | - |
Leu-Leu-Glu-4-methylcoumaryl-7-amide | GluSE-WP, W185, V188, P189 | Staphylococcus epidermidis | |
| 3.4.21.19 | 8863 | - |
Leu-Leu-Glu-4-methylcoumaryl-7-amide | GluSE-W, W185, V188, D189 | Staphylococcus epidermidis | |
| 3.4.21.19 | 9059 | - |
Leu-Leu-Glu-4-methylcoumaryl-7-amide | GluSE-WAP, W185, A188, P189 | Staphylococcus epidermidis | |
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