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Information on EC 3.4.22.48 - staphopain and Organism(s) Staphylococcus aureus and UniProt Accession P0C1S6
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3.4.22.48 staphopainSpecify your search results
Word Map
- 3.4.22.48
- aureus
-
staphylococcal
- streptococcal
- pyogenes
- staphostatins
- speb
-
exotoxin
-
pyrogenic
- aureolysin
- sspc
- gordonii
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Staphylococcus aureus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
staphopain a, extracellular cysteine protease, staphopain, staphopain b, sspb protein, staphopain c, sscp a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SCPA
SspB
staphopain A
staphopain B
staphylopain
staphopain B
-
-
staphylopain
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
mechanism
-
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
active site structure
-
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
active site and substrate binding subsite structures
-
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
active site structure and topology of ScpA
-
CAS REGISTRY NUMBER
COMMENTARY
347841-89-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
-
-
?
cystatin C + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide + H2O
?
-
-
-
-
?
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide + H2O
?
-
-
-
-
?
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
-
-
-
?
5-carboxyfluorescein-Lys-Lys-Ala-Ala-Glu-Ala-Ser-Lys-(QXL520)-OH + H2O
?
-
substrate for ScpA
-
-
?
alcohol dehydrogenase + H2O
alcohol dehydrogenase proteolytically cleaved into peptide fragments
-
-
-
-
?
alpha1-proteinase inhibitor + H2O
?
-
human protein, inactivation by SspA
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
Bz-Pro-Phe-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
casein + H2O
casein proteolytically cleaved into peptide fragments
-
-
-
-
?
CXCR2 + H2O
?
-
the enzyme specifically cleaves the N-terminal domain of human CXCR2 between asparate-35 and alanine-36
-
-
?
elastin + H2O
elastin proteolytically cleaved into peptide fragments
-
insoluble substrate
-
-
?
hemoglobin + H2O
hemoglobin proteolytically cleaved into peptide fragments
-
-
-
-
?
N-benzyloxycarbonyl-Phe-Leu-Glu-NH-p-nitroanilide + H2O
N-benzyloxycarbonyl-Phe-Leu-Glu + p-nitroaniline
-
-
-
-
?
N-Suc-Gly-Phe-Gly-p-nitroanilide + H2O
N-Suc-Gly-Phe-Gly + p-nitroaniline
-
characterization of a staphopain (StpA2aur CH-91) and its inhibitor (StpinA2aur CH-91) from a novel staphylococcal thiol protease operon (stpAB2CH-91), substrate used for inhibition studies
-
-
?
Z-Phe-Leu-Glu-p-nitroanilide + H2O
Z-Phe-Leu-Glu + p-nitroaniline
-
-
-
?
cystatin C + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin C + H2O
?
Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair function as protease inhibitor
-
-
?
cystatin D + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
Ala10 bond hydrolyzed by staphopain A, truncation shown to impair inhibition of additional targets
-
-
?
fibrinogen A alpha chain + H2O
?
-
rather slow degradation through Sscp A
-
-
?
fibrinogen A alpha chain + H2O
?
-
Sscp B cleaves the fibrinogen A alpha-chain at the C-terminal region very efficiently
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity
-
-
?
Galectin-3 + H2O
?
the enzyme inactivates galectin-3, abrogating its stimulation of oxygen radical production in human neutrophils and increasing tissue damage during skin infection
-
-
?
kininogen + H2O
kinin + ?
-
activation of human protein by SspA, kinin generation is responsible for infection associated pain and endema
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
broad specificity
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
broad specificity
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
enzyme may play a role in growth regulation
-
-
?
additional information
?
-
-
staphopains A and B are cysteine proteases, staphopain shows no activity with casein
-
-
?
additional information
?
-
staphopain B shown as a potent trigger of chemerin, the tazarotene-induced gene 2 protein TIG2, normally acting as a ligand for the G-protein coupled receptor CMKLR1, activation shown by proteolytic cleavage of the C-terminus
-
-
?
additional information
?
-
-
staphopain B shown as a potent trigger of chemerin, the tazarotene-induced gene 2 protein TIG2, normally acting as a ligand for the G-protein coupled receptor CMKLR1, activation shown by proteolytic cleavage of the C-terminus
-
-
?
additional information
?
-
-
staphopain A does not cleave human CXCR1
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
-
-
?
cystatin C + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
CXCR2 + H2O
?
-
the enzyme specifically cleaves the N-terminal domain of human CXCR2 between asparate-35 and alanine-36
-
-
?
cystatin C + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
kininogen + H2O
kinin + ?
-
activation of human protein by SspA, kinin generation is responsible for infection associated pain and endema
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity
-
-
?
Galectin-3 + H2O
?
the enzyme inactivates galectin-3, abrogating its stimulation of oxygen radical production in human neutrophils and increasing tissue damage during skin infection
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
broad specificity
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
broad specificity
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
enzyme may play a role in growth regulation
-
-
?
additional information
?
-
staphopain B shown as a potent trigger of chemerin, the tazarotene-induced gene 2 protein TIG2, normally acting as a ligand for the G-protein coupled receptor CMKLR1, activation shown by proteolytic cleavage of the C-terminus
-
-
?
additional information
?
-
-
staphopain B shown as a potent trigger of chemerin, the tazarotene-induced gene 2 protein TIG2, normally acting as a ligand for the G-protein coupled receptor CMKLR1, activation shown by proteolytic cleavage of the C-terminus
-
-
?
additional information
?
-
-
staphopain A does not cleave human CXCR1
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
not affected by changes in ionic strength by changing NaCl concentration
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-trans-epoxysuccinyl-leucylamide-(4-guanido)-butane
-
E-64, irreversible inhibitor
squamous cell carcinoma antigen 1
-
the high association rate constant (kass) for inhibitory complex formation (19000 M/s for staphopain A interaction with SCCA1) suggests that squamous cell carcinoma antigen 1 (SCCA1) can regulate staphopain activity in vivo at epithelial surfaces infected/colonized by Staphylococcu aureus
-
squamous cell carcinoma antigen 1
-
the high association rate constant (kass) for inhibitory complex formation (58000 M/s for staphopain A interaction with SCCA1) suggests that squamous cell carcinoma antigen 1 (SCCA1) can regulate staphopain activity in vivo at epithelial surfaces infected/colonized by Staphylococcu aureus
-
staphostatin A
-
i.e. ScpB, intracellular, endogenous specific inhibitor of ScpA forming noncovalent complexes, structure determination, slight cleaving of the inhibitor by the enzyme
-
staphostatin B
-
structural interactions between inhibitor and enzyme are resolved from crystal structure of the enzyme-inhibitor complex
-
staphostatin B
-
endogenous inhibitor of cysteine proteases, recombinantly expressed in Escherichia coli as wild-type protein and mutant and purified
-
staphostatin B
-
i.e. SspC, intracellular, endogenous specific inhibitor of SspB forming noncovalent complexes, structure determination, slight cleaving of the inhibitor by the enzyme
-
staphostatins
-
co-expression of staphopain and inhibitor staphostatin from the same operon, regulatory effect
-
staphostatins
-
endogenous proteins that specifically inhibit staphopain
-
additional information
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
-
additional information
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
-
additional information
-
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
-
additional information
-
no inhibition by human kininogens and cystatin C
-
additional information
-
the proregion of the zymogen is inhibitory for the mature enzyme
-
additional information
-
inhibitory interactions among staphopains and staphostatins analyzed, inhibitor derived from one species of Staphylococcus can inhibit the staphopain from another species, in vivo assessment of inhibitory activities, inhibitory activities and stoichiometry presented
-
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
-
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
-
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
-
additional information
-
immunglobulin G and immunglobulin G's Fc fragment reduce the effect of SspB
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
-
3.3
N-Suc-Gly-Phe-Gly-p-nitroanilide
-
used as substrate for staphopain inhibition studies
0.0076
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.1639
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.271
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain C
0.014
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain C
0.5871
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.612
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.0056
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.154
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.385
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
N-Suc-Gly-Phe-Gly-p-nitroanilide
-
used for inhibition studies of staphopain identified from a novel staphylococcal thiol protease operon stpAB2CH-91
0.002
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain C
0.056
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.886
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.012
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.032
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.089
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain C
0.0112
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.023
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain C
0.716
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, value below 0.1, staphopain C
3.4
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
118
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.1
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, value below 0.1, staphopain A
62.4
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain C
0.1
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, value below 0.1, staphopain C
0.7
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
127.8
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
consequences of N-terminal truncation of cystatin C for normal inhibitor function summarized
-
additional information
additional information
consequences of N-terminal truncation of cystatin C for normal inhibitor function summarized
-
additional information
additional information
-
consequences of N-terminal truncation of cystatin C for normal inhibitor function summarized
-
additional information
additional information
consequences of N-terminal truncation of cystatin C for normal inhibitor function summarized
-
additional information
additional information
consequences of N-terminal truncation of cystatin C for normal inhibitor function summarized
-
additional information
additional information
-
consequences of N-terminal truncation of cystatin C for normal inhibitor function summarized
-
additional information
additional information
-
inhibitory interactions among staphopains and staphostatins determined
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
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
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.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
physiological function
physiological function
-
both staphopains (staphopain A and staphopain B) prolong the partial thromboplastin time of plasma in a dose- and activity-dependent manner, with SspB being 3fold more potent than ScpA. Staphopains also prolong the thrombin time of both plasma and fibrinogen, indicating that these enzymes can cause impaired plasma clotting through fibrinogen degradation
physiological function
-
staphopain A inhibits CXCR2-dependent neutrophil activation and chemotaxis
physiological function
-
staphopains SspB and ScpA modulate Staphylococcus aureus biofilm integrity. ScpA enzyme has a conserved ability to inhibit biofilm formation
physiological function
SspB is a virulence factor. Its function is dependent on the presence of galectin-3. It inactivates galectin-3, abrogating its stimulation of oxygen radical production in human neutrophils and increasing tissue damage during skin infection. The enzyme is an inhibitor of galectin-3-mediated ROS production
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
analysis of structure and fold of the proenzyme, including the propeptide, interactions between the propeptide and the mature enzyme, modeling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the enzyme staphopain B is synthesized as preproenzyme, the prefragment is cleaved resulting in the proenzyme, after secretion the proenzyme is proteolytically activated to the mature enzyme
additional information
-
staphopain is synthesized as proenzyme, which is processed to the mature form by cleavage of the N-terminally propeptide, interactions between the propeptide and the mature enzyme, modeling, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determination of staphopain A in complex with inhibitor E64, folding pattern
-
inactive mutant staphopain B in complex with inhibitor staphostatin B, 21°C, vapour diffusion method with sitting drops, reservoir solution: 2 M ammonium sulfate, 5% isopropanol, 0.8% v/v 1 M guanidinium hydrochloride, 1-2 weeks, cryoprotection in buffer containing a 9:1 mixture of 2.8 M ammonium sulfate and (2R,3R)-(-)-2,3-butanediol, injected into the drops, X-ray structure determination
-
purified recombinant mature staphopain B, sitting drop vapour diffusion method at 4°C or 21°C, equal volume of protein solution containing 15 mg/ml protein in 5mM Tris, pH 7.5, and reservoir solution containing 50 mM Bis-Tris, pH 6.5, 20% w/v PEG 4000, or 100 mM HEPES, pH 7.5, 21% w/v PEG 4000, and 10% v/v 2-propanol, are mixed, a few weeks, X-ray diffraction structure determination and analysis at 2.5-2.8 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
exchange of active site cysteine residue for an alanine, inactive mutant, fusion to N-terminal His-tag
additional information
-
construction of an inactive mutant, active site mutation of staphopain A results in abrogation of production of both co-expressed proteins
additional information
-
inactivation of gene sspA by transposon insertion exertes a polar effect on genes sspB and sspC expression, the inactivation of all three genes results in attenuation of virulence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ion-exchange chromatography, gelfiltration, immobilized metal ion affinity chromatography for His-tagged protein
recombinant co-expressed His-tagged staphopain A and inhibitor staphostatin A from Escherichia coli strain BL21(DE3) inclusion bodies by refolding and nickel affinity chromatography, method optimization
-
recombinant GST-fusion prostaphopain B from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, gel filtration, and cleavage of the GST-tag followed by ultrafiltration
-
recombinant proenzyme form as GST-fusion protein from Escherichia coli, affinity chromatography, cleavage by V8 proteases to mature enzyme form
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of His-tagged staphopain A and its inhibitor staphostatin A in Escherichia coli strain BL21(DE3) in inclusion bodies, recombinant enzyme is toxic for Escherichia coli cells, therefore a co-expression with the enzyme inhibitor is required for recombinant enzyme production, method optimization
-
expressed in Escherichia coli
expression of large amounts of active wild-type enzyme in Escherichia coli is not possible, probably due to toxicity for the host
-
expression of wild-type enzyme as fusion protein in Escherichia coli, hybrid construct with a N-terminal GST-moiety linked to the proenzyme via a thrombin cleavable linker
-
overexpressed in Staphylococcus aureus, His-tagged version expressed in Escherichia coli
overexpression of the inactive mutant in Escherichia coli BL21(DE3) as His-tagged protein
-
prostaphopain B, expression as GST-fusion protein in Escherichia coli strain BL21(DE3)
-
ssp and scp operons, genomic organization of ssp and scp genes, overview, overexpression of scp operon genes in Escherichia coli
-
Staphylococcus aureus UAMS-1 and its isogenic sarA, agr, and sarA agr regulatory mutant. ScpA is higher in abundance in the sarA and sarA agr mutants than in strain UAMS-1. Analysis of time-dependent ScpA amount during strain cultivation.
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant co-expressed His-tagged staphopain A and inhibitor staphostatin A from Escherichia coli strain BL21(DE3) inclusion bodies by treatment with 6 M guanidinium hydrochloride, and dilution in buffer, at pH 6.0, with 40% glycerol content or with arginine and Tween 20 supplementation, method optimization
-
using 50 mM sodium phosphate, 150 mM sodium chloride, 1 mM EDTA, 0.5 M arginine (pH 6.0), 30% (v/v) glycerol, 1 mM 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
studies on development of therapeutic agents directed toward proteolytic virulence factors
medicine
studies on ability of staphopain B of Staphylococcus aureus to elicit and maintain a chronic inflammatory state, staphopain B suggested to mediate recruitment of specialized host cells, including immunoregulatory plasmacytoid dendritic cells and/or macrophages
pharmacology
studies on development of therapeutic agents directed toward proteolytic virulence factors
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Filipek, R.; Rzychon, M.; Oleksy, A.; Gruca, M.; Dubin, A.; Potempa, J.; Bochtler, M.
The staphostatin-staphopain complex: A forward binding inhibitor in complex with its target cysteine protease
J. Biol. Chem.
278
40959-40966
2003
Staphylococcus aureus
Potempa, J.; Dubin, A.; Travis, J.
Staphylopain
Handbook of Proteolytic Enzymes (Barrett, A. ; Rawlings, N. D. ; Woessner, J. F. eds. )
669-671
1998
Staphylococcus aureus, Staphylococcus aureus V8
-
Rzychon, M.; Sabat, A.; Kosowska, K.; Potempa, J.; Dubin, A.
Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases
Mol. Microbiol.
49
1051-1066
2003
Staphylococcus aureus
Hofmann, B.; Hecht, H.J.; Kiess, M.; Schomburg, D.
Crystal structure of a thiol proteinase from Staphylococcus aureus V8 in the E-64 inhibitor complex
Acta Crystallogr. Sect. A
49
102
1993
Staphylococcus aureus, Staphylococcus aureus V8
-
Dubin, G.
Defense against own arms: staphylococcal cysteine proteases and their inhibitors
Acta Biochim. Pol.
50
715-724
2003
Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus warneri
Wladyka, B.; Puzia, K.; Dubin, A.
Efficient co-expression of a recombinant staphopain A and its inhibitor staphostatin A in Escherichia coli
Biochem. J.
385
181-187
2005
Staphylococcus aureus
Filipek, R.; Szczepanowski, R.; Sabat, A.; Potempa, J.; Bochtler, M.
Prostaphopain B structure: a comparison of proregion-mediated and staphostatin-mediated protease inhibition
Biochemistry
43
14306-14315
2004
Staphylococcus aureus, Staphylococcus aureus V8
Dubin, G.; Wladyka, B.; Stec-Niemczyk, J.; Chmiel, D.; Zdzalik, M.; Dubin, A.; Potempa, J.
The staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity
Biol. Chem.
388
227-235
2007
Staphylococcus aureus, Staphylococcus aureus CH-91, Staphylococcus epidermidis, Staphylococcus warneri
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
Biol. Chem.
388
437-446
2007
Staphylococcus aureus (P0C1S6), Staphylococcus aureus (P81297), Staphylococcus aureus, Staphylococcus aureus V8 (P0C1S6), Staphylococcus aureus V8 (P81297)
Kulig, P.; Zabel, B.A.; Dubin, G.; Allen, S.J.; Ohyama, T.; Potempa, J.; Handel, T.M.; Butcher, E.C.; Cichy, J.
Staphylococcus aureus-derived staphopain B, a potent cysteine protease activator of plasma chemerin
J. Immunol.
178
3713-3720
2007
Staphylococcus aureus (Q2FZL3), Staphylococcus aureus, Staphylococcus aureus NCTC 8325 (Q2FZL3)
Smagur, J.; Guzik, K.; Bzowska, M.; Kuzak, M.; Zarebski, M.; Kantyka, T.; Walski, M.; Gajkowska, B.; Potempa, J.
Staphylococcal cysteine protease staphopain B (SspB) induces rapid engulfment of human neutrophils and monocytes by macrophages
Biol. Chem.
390
361-371
2009
Staphylococcus aureus
Jones, R.C.; Deck, J.; Edmondson, R.D.; Hart, M.E.
Relative quantitative comparisons of the extracellular protein profiles of Staphylococcus aureus UAMS-1 and its sarA, agr, and sarA agr regulatory mutants using one-dimensional polyacrylamide gel electrophoresis and nanocapillary liquid chromatography cou
J. Bacteriol.
190
5265-5278
2008
Staphylococcus aureus
Smagur, J.; Guzik, K.; Magiera, L.; Bzowska, M.; Gruca, M.; Thogersen, I.B.; Enghild, J.J.; Potempa, J.
A new pathway of staphylococcal pathogenesis: apoptosis-like death induced by Staphopain B in human neutrophils and monocytes
J. Innate Immun.
1
98-108
2009
Staphylococcus aureus, Staphylococcus aureus BC10
Nickerson, N.; Ip, J.; Passos, D.T.; McGavin, M.J.
Comparison of Staphopain A (ScpA) and B (SspB) precursor activation mechanisms reveals unique secretion kinetics of proSspB (Staphopain B), and a different interaction with its cognate Staphostatin, SspC
Mol. Microbiol.
75
161-177
2010
Staphylococcus aureus, Staphylococcus aureus (Q2G2R8)
Kalinska, M.; Kantyka, T.; Greenbaum, D.C.; Larsen, K.S.; Wladyka, B.; Jabaiah, A.; Bogyo, M.; Daugherty, P.S.; Wysocka, M.; Jaros, M.; Lesner, A.; Rolka, K.; Schaschke, N.; Stennicke, H.; Dubin, A.; Potempa, J.; Dubin, G.
Substrate specificity of Staphylococcus aureus cysteine proteases - Staphopains A, B and C
Biochimie
94
318-327
2012
Staphylococcus aureus
Kantyka, T.; Plaza, K.; Koziel, J.; Florczyk, D.; Stennicke, H.R.; Thogersen, I.B.; Enghild, J.J.; Silverman, G.A.; Pak, S.C.; Potempa, J.
Inhibition of Staphylococcus aureus cysteine proteases by human serpin potentially limits staphylococcal virulence
Biol. Chem.
392
483-489
2011
Staphylococcus aureus
Ohbayashi, T.; Irie, A.; Murakami, Y.; Nowak, M.; Potempa, J.; Nishimura, Y.; Shinohara, M.; Imamura, T.
Degradation of fibrinogen and collagen by staphopains, cysteine proteases released from Staphylococcus aureus
Microbiology
157
786-792
2011
Staphylococcus aureus
Laarman, A.J.; Mijnheer, G.; Mootz, J.M.; van Rooijen, W.J.; Ruyken, M.; Malone, C.L.; Heezius, E.C.; Ward, R.; Milligan, G.; van Strijp, J.A.; de Haas, C.J.; Horswill, A.R.; van Kessel, K.P.; Rooijakkers, S.H.
Staphylococcus aureus staphopain A inhibits CXCR2-dependent neutrophil activation and chemotaxis
EMBO J.
31
3607-3619
2012
Staphylococcus aureus, Staphylococcus aureus MRSA
Mootz, J.M.; Malone, C.L.; Shaw, L.N.; Horswill, A.R.
Staphopains modulate Staphylococcus aureus biofilm integrity
Infect. Immun.
81
3227-3238
2013
Staphylococcus aureus, Staphylococcus aureus AH1263
Elmwall, J.; Kwiecinski, J.; Na, M.; Ali, A.A.; Osla, V.; Shaw, L.N.; Wang, W.; Saevman, K.; Josefsson, E.; Bylund, J.; Jin, T.; Welin, A.; Karlsson, A.
Galectin-3 is a target for proteases involved in the virulence of Staphylococcus aureus
Infect. Immun.
85
e00177-17
2017
Staphylococcus aureus (Q2FZL3), Staphylococcus aureus (Q2G2R8), Staphylococcus aureus, Staphylococcus aureus NCTC 8325 (Q2FZL3), Staphylococcus aureus NCTC 8325 (Q2G2R8)
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