3.4.22.48: staphopain
This is an abbreviated version!
For detailed information about staphopain, go to the full flat file.
Word Map on EC 3.4.22.48
-
3.4.22.48
-
aureus
-
staphylococcal
-
streptococcal
-
pyogenes
-
staphostatins
-
speb
-
exotoxin
-
pyrogenic
-
aureolysin
-
sspc
-
gordonii
-
pharmacology
-
medicine
- 3.4.22.48
- aureus
-
staphylococcal
- streptococcal
- pyogenes
- staphostatins
- speb
-
exotoxin
-
pyrogenic
- aureolysin
- sspc
- gordonii
- pharmacology
- medicine
Reaction
broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate =
Synonyms
Ecp, extracellular cysteine protease, SCPA, Sscp A, Sscp B, SspB, SspB protein, staphopain, staphopain A, staphopain B, staphopain C, staphylopain
ECTree
3.4.22.48 staphopainAdvanced search results
results (
results (Specific Activity
Specific Activity on EC 3.4.22.48 - staphopain
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SPECIFIC ACTIVITY [µmol/min/mg] 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
additional information
additional information
-
cloning and characterization of staphopain A2 and its inhibitor from a novel staphylococcal thiol protease operon (stpAB2CH-91), staphopain/staphostatin interaction and evolution of encoding operons analyzed, evidence of ancestral allelic duplication and parallel evolution of the protease/inhibitor pairs suggested
additional information
cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by bacterial staphopains described, enzyme kinetic parameters shown
additional information
cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by bacterial staphopains described, enzyme kinetic parameters shown
additional information
-
cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by bacterial staphopains described, enzyme kinetic parameters shown
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
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
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
additional information
proteolytic cleavage of the C-terminus of chemerin, the tazarotene-induced gene 2 protein TIG2, by staphopain B determined by SDS-PAGE, HPLC-analysis and MALDI-TOF, cell-activating potential of chemerin cleavage products determined, clinical isolates of Staphylococcus aureus shown to activate chemerin, activation determined in the presence of plasma inhibitors, no activation of chemerin by staphopain B mutants observed
additional information
-
proteolytic cleavage of the C-terminus of chemerin, the tazarotene-induced gene 2 protein TIG2, by staphopain B determined by SDS-PAGE, HPLC-analysis and MALDI-TOF, cell-activating potential of chemerin cleavage products determined, clinical isolates of Staphylococcus aureus shown to activate chemerin, activation determined in the presence of plasma inhibitors, no activation of chemerin by staphopain B mutants observed
additional information
-
peripheral blood neutrophils and monocytes exposed to SspB are extensively phagocytosed by resting human monocyte-derived macrophages in a time- and concentration-dependent manner. SspB-treated neutrophils engulfed in phagosomesstill preserve mitochondrial potential. SspB blocks phagocytosis of opsonised Staphylococcus aureus by neutrophils and monocytes. SspB blocks the chemotactic activity of neutrophils. SspB decreases surface expression of the major repulsion signal CD31 on neutrophils both in the absence and presence of human serum.
additional information
-
purified enzyme, spectrophotometrical assay
additional information
-
staphopain A of Staphylococcus epidermidis used for assessment of staphopain-staphostatin interactions, kinetics shown
additional information
-
ability of staphostatins to form a complex with the active site mutant C21A of Staphylococcus warneri staphopain determined by size exclusion chromatography
