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Literature summary extracted from

  • Park, J.W.; Park, J.E.; Park, J.K.; Lee, J.S.
    Purification and biochemical characterization of a novel glutamyl endopeptidase secreted by a clinical isolate of Staphylococcus aureus (2011), Int. J. Mol. Med., 27, 637-645.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.19 expressed in Escherichia coli Staphylococcus aureus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.19 diisopropyl fluorophosphate
-
Staphylococcus aureus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.19 1.48
-
L-Phe-L-Leu-L-Glu-4-nitroanilide pH and temperature not specified in the publication 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 prothrombin + H2O Staphylococcus aureus the enzyme preferentially cleaves peptide bonds at the carboxyl sides of glutamate residues in prothrombin ?
-
?
3.4.21.19 prothrombin + H2O Staphylococcus aureus C-66 the enzyme preferentially cleaves peptide bonds at the carboxyl sides of glutamate residues in prothrombin ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.19 Staphylococcus aureus
-
-
-
3.4.21.19 Staphylococcus aureus C-66
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.19
-
Staphylococcus aureus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.19 L-Phe-L-Leu-L-Glu-4-nitroanilide + H2O i.e. L-2135 Staphylococcus aureus L-Phe-L-Leu-L-Glu + 4-nitroaniline
-
?
3.4.21.19 L-Phe-L-Leu-L-Glu-4-nitroanilide + H2O i.e. L-2135 Staphylococcus aureus C-66 L-Phe-L-Leu-L-Glu + 4-nitroaniline
-
?
3.4.21.19 prothrombin + H2O the enzyme preferentially cleaves peptide bonds at the carboxyl sides of glutamate residues in prothrombin Staphylococcus aureus ?
-
?
3.4.21.19 prothrombin + H2O the enzyme preferentially cleaves peptide bonds at the carboxyl sides of glutamate residues in prothrombin Staphylococcus aureus C-66 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.19 glutamate-specific serine endopeptidase
-
Staphylococcus aureus
3.4.21.19 VSPase
-
Staphylococcus aureus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.19 45
-
-
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 44.4
-
L-Phe-L-Leu-L-Glu-4-nitroanilide pH and temperature not specified in the publication Staphylococcus aureus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.19 6 8.5
-
Staphylococcus aureus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.4.21.19 30
-
L-Phe-L-Leu-L-Glu-4-nitroanilide pH and temperature not specified in the publication Staphylococcus aureus