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Information on EC 3.4.22.48 - staphopain
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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 enzyme appears in viruses and cellular organisms
Synonyms
staphopain a, extracellular cysteine protease, staphopain, staphopain b, sspb protein, staphopain c, sscp a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SCPA
SspB
SspB protein
staphopain A
staphopain B
staphylopain
staphopain B
-
-
staphylopain
-
-
-
-
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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
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
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
-
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
-
-
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CAS REGISTRY NUMBER
COMMENTARY
347841-89-8
-
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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
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
?
-
-
-
-
?
alcohol dehydrogenase + H2O
alcohol dehydrogenase proteolytically cleaved into peptide fragments
alpha-1-antitrypsin + H2O
alpha-1-antitrypsin proteolytically cleaved into peptide fragments
-
limited proteolysis
-
-
?
alpha1-proteinase inhibitor + H2O
?
-
human protein, inactivation by SspA
-
-
?
elastin + H2O
elastin proteolytically cleaved into peptide fragments
-
insoluble substrate
-
-
?
HMW-kininogen + H2O
HMW-kininogen proteolytically cleaved into peptide fragments
-
limited proteolysis
-
-
?
N-benzyloxycarbonyl-Phe-Leu-Glu-NH-p-nitroanilide + H2O
N-benzyloxycarbonyl-Phe-Leu-Glu + p-nitroaniline
-
-
-
-
?
Z-Phe-Leu-Glu-p-nitroanilide + H2O
Z-Phe-Leu-Glu + p-nitroaniline
-
-
-
?
5-carboxyfluorescein-Lys-Lys-Ala-Ala-Glu-Ala-Ser-Lys-(QXL520)-OH + H2O
?
-
substrate for ScpA
-
-
?
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
-
-
-
-
?
alcohol dehydrogenase + H2O
alcohol dehydrogenase proteolytically cleaved into peptide fragments
-
-
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
?
-
substrate for SspB
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
Bz-Pro-Phe-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
Bz-Pro-Phe-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
casein + H2O
casein proteolytically cleaved into peptide fragments
-
-
-
-
?
casein + H2O
casein proteolytically cleaved into peptide fragments
-
-
-
-
?
Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
-
-
?
CXCR2 + H2O
?
-
the enzyme specifically cleaves the N-terminal domain of human CXCR2 between asparate-35 and alanine-36
-
-
?
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 C + H2O
?
Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair function as protease inhibitor
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity
-
-
?
hemoglobin + H2O
hemoglobin proteolytically cleaved into peptide fragments
-
-
-
-
?
hemoglobin + H2O
hemoglobin proteolytically cleaved into peptide fragments
-
-
-
-
?
kininogen + H2O
kinin + ?
-
activation of human protein by SspA, kinin generation is responsible for infection associated pain and endema
-
-
?
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
-
-
?
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
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
broad specificity
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
-
-
-
?
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
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
-
-
-
?
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
-
-
?
additional information
?
-
-
staphopain A does not cleave human CXCR1
-
-
?
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
?
-
-
inhibitory interactions among staphopains and staphostatins determined, staphopain A of Staphylococcus epidermidis purified and used for interaction analysis
-
-
?
additional information
?
-
-
inhibitory interactions among staphopains and staphostatins determined and used for interaction analysis
-
-
?
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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
-
-
?
kininogen + H2O
kinin + ?
-
activation of human protein by SspA, kinin generation is responsible for infection associated pain and endema
-
-
?
CXCR2 + H2O
?
-
the enzyme specifically cleaves the N-terminal domain of human CXCR2 between asparate-35 and alanine-36
-
-
?
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 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
-
-
?
cystatin D + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
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
-
-
?
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
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
broad specificity
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
-
-
-
?
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
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
-
-
-
?
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
-
-
?
additional information
?
-
-
staphopain A does not cleave human CXCR1
-
-
?
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
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
not affected by changes in ionic strength by changing NaCl concentration
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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; 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
-
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
-
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
-
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; 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 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
-
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
-
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
-
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
-
staphostin homologue genes are probably encoding enzyme inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Bone Resorption
Characteristics of C-terminal, ?-amyloid peptide binding fragment of neuroprotective protease inhibitor, cystatin C.
Dermatitis, Atopic
Identification of bacterial biofilm and the Staphylococcus aureus derived protease, staphopain, on the skin surface of patients with atopic dermatitis.
Infections
An amino-terminal signal peptide of Vfr protein negatively influences RopB-dependent SpeB expression and attenuates virulence in Streptococcus pyogenes.
Infections
Extracellular cysteine protease produced by Streptococcus pyogenes participates in the pathogenesis of invasive skin infection and dissemination in mice.
Infections
Intracellular Staphylococcus aureus employs the cysteine protease staphopain A to induce host cell death in epithelial cells.
Infections
Replacement of histidine 340 with alanine inactivates the group A Streptococcus extracellular cysteine protease virulence factor.
Lung Neoplasms
Enriched SSCP: a highly sensitive method for the detection of unknown mutations. Application to the molecular diagnosis of lung cancer in sputum samples.
Neoplasms
Cystatin C properties crucial for uptake and inhibition of intracellular target enzymes.
Neoplasms
Enriched SSCP: a highly sensitive method for the detection of unknown mutations. Application to the molecular diagnosis of lung cancer in sputum samples.
Neoplasms
Extracellular protease imaging for cell mass tracking of xenografted human malignant pleural mesothelioma.
Pneumonia
Intracellular Staphylococcus aureus employs the cysteine protease staphopain A to induce host cell death in epithelial cells.
Soft Tissue Infections
Replacement of histidine 340 with alanine inactivates the group A Streptococcus extracellular cysteine protease virulence factor.
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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
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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