Application | Comment | Organism |
---|---|---|
pharmacology | studies on development of therapeutic agents directed toward proteolytic virulence factors | Staphylococcus aureus |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli | Staphylococcus aureus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | no inhibition of the cysteine proteases staphopain A by cystatin A, C, D and cystatin E/M, inhibitors shown to be hydrolyzed by staphopain A, inhibitory activity of native and staphopain-generated modified forms of cystatins presented; no inhibition of the cysteine proteases staphopain B by cystatin A, C, D and cystatin E/M, inhibitory activity of native and staphopain-generated modified forms of cystatins presented | Staphylococcus aureus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.032 | - |
cystatin D | Ala10 bond hydrolyzed by staphopain A, truncation of cystatin D shown to cause alleviated inhibition of endogenous target enzymes investigated, disturbance of the host protease-inhibitor balance | Staphylococcus aureus | |
0.033 | - |
cystatin C | Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair inhibition of additional targets, disturbance of the host protease-inhibitor balance | Staphylococcus aureus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | secreted, culture supernatant | Staphylococcus aureus | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
cystatin C + H2O | Staphylococcus aureus | specificity of staphopains when interacting with cystatins as natural protein substrates presented | ? | - |
? | |
cystatin C + H2O | Staphylococcus aureus V8 | specificity of staphopains when interacting with cystatins as natural protein substrates presented | ? | - |
? | |
cystatin D + H2O | Staphylococcus aureus | specificity of staphopains when interacting with cystatins as natural protein substrates presented | ? | - |
? | |
cystatin D + H2O | Staphylococcus aureus V8 | specificity of staphopains when interacting with cystatins as natural protein substrates presented | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | P0C1S6 | staphopain B; V8 strain | - |
Staphylococcus aureus | P81297 | staphopain A; V8 strain | - |
Staphylococcus aureus V8 | P0C1S6 | staphopain B; V8 strain | - |
Staphylococcus aureus V8 | P81297 | staphopain A; V8 strain | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
culture medium | purified from | Staphylococcus aureus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by bacterial staphopains described, enzyme kinetic parameters shown | Staphylococcus aureus |
additional information | - |
MALDI-TOF based time-course experiments of cleavage of cystatin C and D by staphopain A indicated, cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by staphopain A described, enzyme kinetic parameters shown | Staphylococcus aureus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cystatin C + H2O | specificity of staphopains when interacting with cystatins as natural protein substrates presented | Staphylococcus aureus | ? | - |
? | |
cystatin C + H2O | Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair function as protease inhibitor | Staphylococcus aureus | ? | - |
? | |
cystatin C + H2O | specificity of staphopains when interacting with cystatins as natural protein substrates presented | Staphylococcus aureus V8 | ? | - |
? | |
cystatin C + H2O | Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair function as protease inhibitor | Staphylococcus aureus V8 | ? | - |
? | |
cystatin D + H2O | specificity of staphopains when interacting with cystatins as natural protein substrates presented | Staphylococcus aureus | ? | - |
? | |
cystatin D + H2O | Ala10 bond hydrolyzed by staphopain A, truncation shown to impair inhibition of additional targets | Staphylococcus aureus | ? | - |
? | |
cystatin D + H2O | specificity of staphopains when interacting with cystatins as natural protein substrates presented | Staphylococcus aureus V8 | ? | - |
? | |
cystatin D + H2O | Ala10 bond hydrolyzed by staphopain A, truncation shown to impair inhibition of additional targets | Staphylococcus aureus V8 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
staphopain A | - |
Staphylococcus aureus |
staphopain B | - |
Staphylococcus aureus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | consequences of N-terminal truncation of cystatin C for normal inhibitor function summarized | Staphylococcus aureus |