Information on EC 3.4.22.48 - staphopain

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The expected taxonomic range for this enzyme is: Staphylococcus

EC NUMBER
COMMENTARY
3.4.22.48
-
RECOMMENDED NAME
GeneOntology No.
staphopain
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
show the reaction diagram
Known from species of Staphylococcus. Type example of peptidase family C47
-
-
-
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
show the reaction diagram
active site structure; 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
show the reaction diagram
active site structure and topology of ScpA
-
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
show the reaction diagram
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
show the reaction diagram
active site and substrate binding subsite structures
Staphylococcus aureus V8
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
extracellular cysteine protease
-
-
SspB protein
Q2FZL3
-
SspB protein
Staphylococcus aureus 8325-4
Q2FZL3
-
-
staphopain
-
-
staphopain A
P81297
-
staphopain A
Q2G2R8
-
staphopain A
Staphylococcus aureus V8
P81297
-
-
staphopain B
P0C1S6
-
staphopain B
Q2FZL3
-
staphopain B
Staphylococcus aureus 8325-4
Q2FZL3
-
-
staphopain B
Staphylococcus aureus BC10, Staphylococcus aureus V8
-
-
-
staphopain B
Staphylococcus aureus V8
P0C1S6
-
-
staphopain B
-
-
staphopain C
-
-
staphylopain
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
347841-89-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzyme might be inducible by elastin in vivo; V8
-
-
Manually annotated by BRENDA team
stain UAMS-1 and and its isogenic sarA, agr and sarA agr regulatory mutants
-
-
Manually annotated by BRENDA team
staphopain A; staphopain B
-
-
Manually annotated by BRENDA team
staphopain A; V8
-
-
Manually annotated by BRENDA team
staphopain A; V8 strain
SwissProt
Manually annotated by BRENDA team
staphopain B
-
-
Manually annotated by BRENDA team
staphopain B; V8 strain
SwissProt
Manually annotated by BRENDA team
strain 8325-4 including isogenic knockout mutants in the 8325-4 genetic background
SwissProt
Manually annotated by BRENDA team
strain BC10
-
-
Manually annotated by BRENDA team
strain CH-91
-
-
Manually annotated by BRENDA team
Staphylococcus aureus 8325-4
strain 8325-4 including isogenic knockout mutants in the 8325-4 genetic background
SwissProt
Manually annotated by BRENDA team
Staphylococcus aureus BC10
strain BC10
-
-
Manually annotated by BRENDA team
Staphylococcus aureus CH-91
strain CH-91
-
-
Manually annotated by BRENDA team
Staphylococcus aureus V8
staphopain A; V8 strain
SwissProt
Manually annotated by BRENDA team
Staphylococcus aureus V8
staphopain B; V8 strain
SwissProt
Manually annotated by BRENDA team
Staphylococcus aureus V8
strain V8
-
-
Manually annotated by BRENDA team
Staphylococcus aureus V8
V8
-
-
Manually annotated by BRENDA team
active-site mutant C21A, derived from strain SW035
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-Glu-Ala-Leu-Gly-Thr-Ser-Pro-Arg-Lys(Dnp)-Asp + H2O
?
show the reaction diagram
-
-
-
-
?
Abz-Glu-Gly-Ile-Gly-Thr-Ser-Arg-Pro-Lys(Dnp)-Asp + H2O
?
show the reaction diagram
-
-
-
-
?
alcohol dehydrogenase + H2O
alcohol dehydrogenase proteolytically cleaved into peptide fragments
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus V8
-
-
-
-
?
alpha-1-antitrypsin + H2O
alpha-1-antitrypsin proteolytically cleaved into peptide fragments
show the reaction diagram
-
limited proteolysis
-
-
?
alpha1-proteinase inhibitor + H2O
?
show the reaction diagram
-
human protein, inactivation by SspA
-
-
?
benzyl-Tyr-OEt + H2O
?
show the reaction diagram
-
-
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
Bz-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus V8
-
chromogenic substrate
-
-
?
casein + H2O
casein proteolytically cleaved into peptide fragments
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus V8
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
cystatin C + H2O
?
show the reaction diagram
P0C1S6, P81297
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin C + H2O
?
show the reaction diagram
P0C1S6, P81297
Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair function as protease inhibitor
-
-
?
cystatin C + H2O
?
show the reaction diagram
Staphylococcus aureus V8
P0C1S6, P81297
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin C + H2O
?
show the reaction diagram
Staphylococcus aureus V8
P0C1S6, P81297
Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair function as protease inhibitor
-
-
?
cystatin D + H2O
?
show the reaction diagram
P0C1S6, P81297
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
show the reaction diagram
P0C1S6, P81297
Ala10 bond hydrolyzed by staphopain A, truncation shown to impair inhibition of additional targets
-
-
?
cystatin D + H2O
?
show the reaction diagram
Staphylococcus aureus V8
P0C1S6, P81297
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
show the reaction diagram
Staphylococcus aureus V8
P0C1S6, P81297
Ala10 bond hydrolyzed by staphopain A, truncation shown to impair inhibition of additional targets
-
-
?
elastin + H2O
elastin proteolytically cleaved into peptide fragments
show the reaction diagram
-
insoluble substrate
-
-
?
fibrinogen A alpha chain + H2O
?
show the reaction diagram
-
rather slow degradation through Sscp A, Sscp B cleaves the fibrinogen A alpha-chain at the C-terminal region very efficiently
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
staphopain B
-
-
?
hemoglobin + H2O
hemoglobin proteolytically cleaved into peptide fragments
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus V8
-
-
-
-
?
HMW-kininogen + H2O
HMW-kininogen proteolytically cleaved into peptide fragments
show the reaction diagram
-
limited proteolysis
-
-
?
integrin CD11b + H2O
?
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus BC10
-
on phagocytes
-
-
?
N-benzyloxycarbonyl-Phe-Leu-Glu-NH-p-nitroanilide + H2O
N-benzyloxycarbonyl-Phe-Leu-Glu + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-Suc-Gly-Phe-Gly-p-nitroanilide + H2O
N-Suc-Gly-Phe-Gly + p-nitroaniline
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus CH-91
-
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
-
-
?
peptide + H2O
amino acids
show the reaction diagram
-
-
-
-
?
peptide + H2O
amino acids
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus V8
-
broad specificity
-
-
?
peptide + H2O
amino acids
show the reaction diagram
Staphylococcus aureus V8
-
-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
show the reaction diagram
-
-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
show the reaction diagram
-
broad specificity
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
show the reaction diagram
Staphylococcus aureus V8
-
-
-
-
?
protein + H2O
peptide fragments
show the reaction diagram
-
-
-
-
?
protein + H2O
peptide fragments
show the reaction diagram
-
-
-
-
?
protein + H2O
peptide fragments
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus V8
-
broad specificity
-
-
?
protein + H2O
peptide fragments
show the reaction diagram
Staphylococcus aureus V8
-
-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
show the reaction diagram
-
-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
show the reaction diagram
-
broad specificity, enzyme may play a role in growth regulation
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
show the reaction diagram
Staphylococcus aureus V8
-
-
-
-
?
Z-Phe-Leu-Glu-p-nitroanilide + H2O
Z-Phe-Leu-Glu + p-nitroaniline
show the reaction diagram
Q2G2R8
-
-
-
?
Kininogen + H2O
Kinin
show the reaction diagram
-
activation of human protein by SspA, kinin generation is responsible for infection associated pain and endema, human protein, activation by SspA
-
-
?
additional information
?
-
-
staphopains A and B are cysteine proteases, staphopain shows no activity with casein
-
-
-
additional information
?
-
Q2FZL3
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
?
-
-
inhibitory interactions among staphopains and staphostatins determined and used for interaction analysis
-
-
-
additional information
?
-
-
inhibitory interactions among staphopains and staphostatins determined, staphopain A of Staphylococcus epidermidis purified and used for interaction analysis
-
-
-
additional information
?
-
Staphylococcus aureus 8325-4
Q2FZL3
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cystatin C + H2O
?
show the reaction diagram
P0C1S6, P81297
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin C + H2O
?
show the reaction diagram
Staphylococcus aureus V8
P0C1S6, P81297
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
show the reaction diagram
P0C1S6, P81297
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
show the reaction diagram
Staphylococcus aureus V8
P0C1S6, P81297
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
integrin CD11b + H2O
?
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus BC10
-
on phagocytes
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
show the reaction diagram
-
-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
show the reaction diagram
-
broad specificity
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
show the reaction diagram
Staphylococcus aureus V8
-
-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
show the reaction diagram
-
-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
show the reaction diagram
-
broad specificity, enzyme may play a role in growth regulation
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
show the reaction diagram
Staphylococcus aureus V8
-
-
-
-
?
Kininogen + H2O
Kinin
show the reaction diagram
-
activation of human protein by SspA, kinin generation is responsible for infection associated pain and endema
-
-
?
additional information
?
-
Staphylococcus aureus, Staphylococcus aureus 8325-4
Q2FZL3
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
not affected by changes in ionic strength by changing NaCl concentration
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
alpha2-Macroglobulin
-
from human
-
alpha2-Macroglobulin
-
from human
-
E-64
-
stochiometrical and irreversible inhibition
E64
-
ScpA-inhibitor binding structure
p-hydroxymercuribenzoate
-
-
phosphorylated cystatin alpha
-
from rat skin
-
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; 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
-
-
-
staphostatin A
-
absolute specific for staphopain A; encoded by the gene scpB
-
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
-
endogenous inhibitor of cysteine proteases, recombinantly expressed in Escherichia coli as wild-type protein and mutant and purified; forms a mixed eight-stranded beta-barrel; structural interactions between inhibitor and enzyme are resolved from crystal structure of the enzyme-inhibitor complex
-
staphostatin B
-
absolute specific for staphopain B; encoded by the gene scpC
-
staphostatin B
-
i.e. SspC, intracellular, endogenous specific inhibitor of SspB forming noncovalent complexes, structure determination, slight cleaving of the inhibitor by the enzyme
-
staphostatin B
-
characterization of an endogenous staphostatin from Staphylococcus warneri and its target protease, in vivo assessment of inhibitory activities tested, inhibitor derived from one species of Staphylococcus can inhibit the staphopain from another species, inhibition only observed if both proteins belong to the same subgroup of either staphopain A/staphostatin A or staphopain B/staphostatin B orthologs
-
staphostatins
-
co-expression of staphopain and inhibitor staphostatin from the same operon, regulatory effect; endogenous proteins that specifically inhibit staphopain; formation of tight and stable non-covalent complexes
-
T-Kininogen
-
from rat
-
L-trans-epoxysuccinyl-leucylamide-(4-guanido)-butane
-
E-64, irreversible inhibitor
additional information
-
no inhibition by human kininogens and cystatin C
-
additional information
-
no inhibition by O-phenanthroline, diisofluorophosphate, phenylmethanesulfonyl fluoride, human kininogens and cystatins A,C, and D
-
additional information
-
staphostin homologue genes are probably encoding enzyme inhibitors
-
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
-
in vivo assessment of inhibitory activities determined, inhibitor derived from one species of Staphylococcus can inhibit the staphopain from another species, inhibition only observed if both proteins belong to the same subgroup of either staphopain A/staphostatin A or staphopain B/staphostatin B orthologs
-
additional information
P0C1S6, P81297
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
-
additional information
-
immunglobulin G and immunglobulin G's Fc fragment reduce the effect of SspB
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
reducing thiol compounds
-
dependent on
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0076
-
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.1639
-
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.271
-
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain C
-
0.014
-
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain C
-
0.5871
-
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.612
-
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.0056
-
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.154
-
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.385
-
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain C
-
0.033
-
cystatin C
P0C1S6, P81297
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
P0C1S6, P81297
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
-
0.5
-
N-benzyloxycarbonyl-Phe-Leu-Glu-NH-p-nitroanilide
-
pH 8.0-8.8
-
3.3
-
N-Suc-Gly-Phe-Gly-p-nitroanilide
-
used as substrate for staphopain inhibition studies
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.002
-
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain C
-
0.056
-
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.886
-
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.012
-
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.032
-
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.089
-
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain C
-
0.0112
-
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.023
-
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain C
-
0.716
-
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
-
0.16
-
N-benzyloxycarbonyl-Phe-Leu-Glu-NH-p-nitroanilide
-
pH 8.0-8.8
-
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
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, value below 0.1, staphopain C
0
3.4
-
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
0
118
-
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
0
0.1
-
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, value below 0.1, staphopain A
0
62.4
-
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain C
0
0.1
-
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, value below 0.1, staphopain C
0
0.7
-
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
0
127.8
-
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37C, staphopain A
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00052
-
E-64
-
pH 8.0-8.8
additional information
-
additional information
-
inhibitory interactions among staphopains and staphostatins determined
-
additional information
-
additional information
-
inhibitory interactions among staphopains and staphostatins indicated, kinetics shown
-
additional information
-
additional information
P0C1S6, P81297
consequences of N-terminal truncation of cystatin C for normal inhibitor function summarized; consequences of N-terminal truncation of cystatin C for normal inhibitor function summarized
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
purified enzyme, spectrophotometrical assay
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
-
-
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
additional information
-
P0C1S6, P81297
cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by bacterial staphopains described, enzyme kinetic parameters shown; 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
-
Q2FZL3
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
substrate insoluble elastin
7
-
-
assay at
7.5
-
-
substrate benzyl-Tyr-OEt
8
8.8
-
substrate casein or hemoglobin
additional information
-
-
pI: 9.4
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
P0C1S6, P81297
purified from; purified from
Manually annotated by BRENDA team
Staphylococcus aureus 8325-4
-
-
-
Manually annotated by BRENDA team
Staphylococcus aureus CH-91
-
purified from
-
Manually annotated by BRENDA team
Staphylococcus aureus V8
-
purified from; purified from
-
Manually annotated by BRENDA team
Staphylococcus aureus V8
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted as zymogen
-
Manually annotated by BRENDA team
P0C1S6, P81297
secreted, culture supernatant; secreted, culture supernatant
-
Manually annotated by BRENDA team
Q2FZL3
isolated from culture medium
-
Manually annotated by BRENDA team
Staphylococcus aureus 8325-4
-
isolated from culture medium
-
-
Manually annotated by BRENDA team
Staphylococcus aureus CH-91
-
secreted, culture supernatant
-
-
Manually annotated by BRENDA team
Staphylococcus aureus V8
-
culture supernatant; secreted, culture supernatant; secreted, culture supernatant
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
13000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 19832, DNA sequence determination
monomer
-
1 * 13000, SDS-PAGE
monomer
Staphylococcus aureus V8
-
1 * 13000, SDS-PAGE
-
additional information
-
analysis of structure and fold of the proenzyme, including the propeptide, interactions between the propeptide and the mature enzyme, modeling, overview
additional information
Staphylococcus aureus V8
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
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
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
Staphylococcus aureus V8
-
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 ACCESSION NO.
LITERATURE
crystal structure determination of staphopain A in complex with inhibitor E64, folding pattern
-
inactive mutant staphopain B in complex with inhibitor staphostatin B, 21C, 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 4C or 21C, 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
-
staphopain A
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; ion-exchange chromatography, gelfiltration, immobilized metal ion affinity chromatography for His-tagged protein
Q2G2R8
cysteine protease StpA2aur CH-91 purified by gel filtration
-
native from culture supernatant
-
native from culture supernatant; recombinant inactive mutant form, His-tagged, from Escherichia coli; recombinant proenzyme form as GST-fusion protein from Escherichia coli, affinity chromatography, cleavage by V8 proteases to mature enzyme form
-
recombinant and native protein, gel filtration
Q2FZL3
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
-
from culture supernatant, apparant homogenity
-
purified by gel filtration
-
recombinant protein, purified by gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
expressed in Escherichia coli; expressed in Escherichia coli
P0C1S6, P81297
expressed in Escherichia coli; overexpressed in Staphylococcus aureus, His-tagged version expressed in Escherichia coli
Q2G2R8
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; 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.
-
DNA and partial amino acid sequence determination and analysis
-
expressed in Escherichia coli
-
ssp and scp operons, genomic organization of ssp and scp genes, overview
-
cysteine protease staphopain B of Staphylococcus warneri transformed into Escherichia coli strain BL21(DE3)pLysS, expression failed, mutant C21A used for recombinant protein production, expression in Escherichia coli strain BL21(DE3)
-
ssp and scp operons, genomic organization of ssp and scp genes, overview
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C21A
-
purification of native staphopain B unsuccessful since strain SW035 produces only minimally detectable protease activity, active-site mutation generated by site-directed mutagenesis, catalytically inactive mutant StpBwar C21A used for interaction studies
additional information
-
exchange of active site cysteine residue for an alanine, inactive mutant, fusion to N-terminal His-tag
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
additional information
-
construction of an inactive mutant, active site mutation of staphopain A results in abrogation of production of both co-expressed proteins
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
Q2FZL3
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
P0C1S6, P81297
studies on development of therapeutic agents directed toward proteolytic virulence factors; studies on development of therapeutic agents directed toward proteolytic virulence factors
medicine
Staphylococcus aureus 8325-4
-
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
Staphylococcus aureus V8
-
studies on development of therapeutic agents directed toward proteolytic virulence factors; studies on development of therapeutic agents directed toward proteolytic virulence factors
-