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Literature summary for 3.4.22.48 extracted from

  • Vincents, B.; Onnerfjord, P.; Gruca, M.; Potempa, J.; Abrahamson, M.
    Down-regulation of human extracellular cysteine protease inhibitors by the secreted staphylococcal cysteine proteases, staphopain A and B (2007), Biol. Chem., 388, 437-446.
    View publication on PubMed

Application

Application Comment Organism
pharmacology studies on development of therapeutic agents directed toward proteolytic virulence factors Staphylococcus aureus

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Staphylococcus aureus

Inhibitors

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 [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

Localization Comment Organism GeneOntology No. Textmining
extracellular secreted, culture supernatant Staphylococcus aureus
-
-

Natural Substrates/ Products (Substrates)

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

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

Source Tissue Comment Organism Textmining
culture medium purified from Staphylococcus aureus
-

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
staphopain A
-
Staphylococcus aureus
staphopain B
-
Staphylococcus aureus

Ki Value [mM]

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