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Literature summary extracted from
- Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli (2008), FEBS J., 275, 573-587.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.21.19 | expressed as soluble His-tag fusion protein in Escherichia coli | Staphylococcus epidermidis |
| 3.4.21.19 | expressed in Escherichia coli, poor expression of native full length protein, successful expression when mature protein sequence is fused with the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, successful expression of double and four point mutant in Escherichia coli | Staphylococcus aureus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.21.19 | DELTA1-48 | the 38 and 40 kDa mature forms are obtained after thermolysin treatment | Staphylococcus aureus |
| 3.4.21.19 | DELTA1-55 | the 38 and 40 kDa mature forms are obtained after thermolysin treatment | Staphylococcus aureus |
| 3.4.21.19 | DELTA1-60 | the 38 and 40 kDa mature forms are obtained after thermolysin treatment | Staphylococcus aureus |
| 3.4.21.19 | DELTA1-62 | the 38 and 40 kDa mature forms are obtained after thermolysin treatment | Staphylococcus aureus |
| 3.4.21.19 | DELTA1-64 | poor expression in Escherichia coli, resulting enzyme thoroughly degraded upon thermolysin treatment, very low activity | Staphylococcus aureus |
| 3.4.21.19 | DELTA1-65 | poor expression in Escherichia coli, resulting enzyme thoroughly degraded upon thermolysin treatment, activity hardly detectable | Staphylococcus aureus |
| 3.4.21.19 | E62Q/E65S | mutation prevent degradation of protein, slightly accelerated proliferation rate compared with wild type enzyme when expressed in Escherichia coli | Staphylococcus aureus |
| 3.4.21.19 | E62Q/E65S/A67P/N68P | efficient suppression of proteolysis, strongly accelerated proliferation rate compared with wild type enzyme when expressed in Escherichia coli | Staphylococcus aureus |
| 3.4.21.19 | additional information | mature protein sequence is fused with the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, suppression of protein degradation, accelerated proliferation rate compared with wild type enzyme when expressed in Escherichia coli | Staphylococcus aureus |
| 3.4.21.19 | S237A | mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, no proteinolytic activity | Staphylococcus aureus |
| 3.4.21.19 | S66R | insertion of a trypsin degradable sequence, successful enzyme processing by trypsin instead of thermolysin, enhanced Glu-specific activity | Staphylococcus aureus |
| 3.4.21.19 | S66R/V69A | insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 4.5% of activity compared with the Val69 native form | Staphylococcus epidermidis |
| 3.4.21.19 | S66R/V69F | insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 1.4% of activity compared with the Val69 native form | Staphylococcus epidermidis |
| 3.4.21.19 | S66R/V69G | insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 1.1% of activity compared with the Val69 native form | Staphylococcus epidermidis |
| 3.4.21.19 | S66R/V69S | insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 0.6% of activity compared with the Val69 native form | Staphylococcus epidermidis |
| 3.4.21.19 | V69A | mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, normal processing of propeptide to mature protein, no proteinolytic activity | Staphylococcus aureus |
| 3.4.21.19 | V69F | mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, normal processing of propeptide to mature protein, no proteinolytic activity | Staphylococcus aureus |
| 3.4.21.19 | V69G | mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, normal processing of propeptide to mature protein, no proteinolytic activity | Staphylococcus aureus |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.19 | 40000 | - |
x * 40000, SDS-PAGE, recombinant full length protein | Staphylococcus aureus |
| 3.4.21.19 | 44000 | - |
x * 44000, SDS-PAGE, recombinant fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, minor species of 42000 Da obtained after purification | Staphylococcus aureus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.19 | GluV8 + H2O | Staphylococcus aureus | degradation of the C-terminus at the Glu279-Asp280 bond is suspected to be a result from autoproteolysis | ? | 38 kDa species | ? |  |
| 3.4.21.19 | additional information | Staphylococcus epidermidis | specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp | ? | - |
? | |
| 3.4.21.19 | additional information | Staphylococcus aureus | specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp, key role in degrading the cell-bound Staphylococcus surface adhesion molecules of fibronectin-binding proteins and protein A | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.19 | Staphylococcus aureus | - |
- |
- |
| 3.4.21.19 | Staphylococcus epidermidis | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.21.19 | proteolytic modification | upon thermolysin treatment the 44 kDa protein is converted to a 42 kDa species and, finally, to 38 and 40 kDa species, degradation of C-terminus at the Glu279-Asp280 bond is suspected to be a result from autoproteolysis | Staphylococcus aureus |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.21.19 | large scale purification as one step purification using Talon affinity chromatography | Staphylococcus epidermidis |
| 3.4.21.19 | recombinant fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis and the four point mutant enzyme in large scale using Talon affinity chromatography | Staphylococcus aureus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.19 | casein + H2O | - |
Staphylococcus aureus | ? | - |
? | |
| 3.4.21.19 | casein + H2O | - |
Staphylococcus epidermidis | ? | - |
? | |
| 3.4.21.19 | GluV8 + H2O | degradation of the C-terminus at the Glu279-Asp280 bond is suspected to be a result from autoproteolysis | Staphylococcus aureus | ? | 38 kDa species | ? | |
| 3.4.21.19 | additional information | specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp | Staphylococcus epidermidis | ? | - |
? | |
| 3.4.21.19 | additional information | specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp, key role in degrading the cell-bound Staphylococcus surface adhesion molecules of fibronectin-binding proteins and protein A | Staphylococcus aureus | ? | - |
? | |
| 3.4.21.19 | Z-Leu-Leu-Glu-MCA + H2O | - |
Staphylococcus aureus | ? | - |
? | |
| 3.4.21.19 | Z-Leu-Leu-Glu-MCA + H2O | - |
Staphylococcus epidermidis | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.19 | ? | mobility of the mature protein on SDS-PAGE is altered by heating the samples, proteins can be fully renaturated under conditions of zymography | Staphylococcus aureus |
| 3.4.21.19 | ? | x * 29000-32000, SDS-PAGE, full length protein | Staphylococcus epidermidis |
| 3.4.21.19 | ? | x * 40000, SDS-PAGE, recombinant full length protein | Staphylococcus aureus |
| 3.4.21.19 | ? | x * 44000, SDS-PAGE, recombinant fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, minor species of 42000 Da obtained after purification | Staphylococcus aureus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.19 | GluSE | enzyme consists of 282 amino acids, composed of a preprosequence (Met1-Ser66) and a mature part (Val67-Gln282) | Staphylococcus epidermidis |
| 3.4.21.19 | GluV8 | - |
Staphylococcus aureus |
| 3.4.21.19 | V8 protease | member of the glutamyl endopeptidase I family, protein of 336 amino acids that includes a prepropeptide consisting of 68 residues (Met1-Asn68) and a C-terminal tail of 52 residues consisting of a 12fold repeat of the tripeptide Pro-Asp/Asn-Asn, prosegment is essential for the suppression of proteolytic activity, as well as for the correct folding of GluV8, indicating its role as an intramolecular chaperone | Staphylococcus aureus |
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