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
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3.4.22.48
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aureus
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staphylococcal
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streptococcal
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pyogenes
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staphostatins
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speb
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exotoxin
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pyrogenic
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aureolysin
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sspc
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gordonii
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pharmacology
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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
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Substrates Products
Substrates Products on EC 3.4.22.48 - staphopain
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REACTION DIAGRAM
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide + H2O
?
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-
-
-
?
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
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limited proteolysis
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-
?
alpha1-proteinase inhibitor + H2O
?
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human protein, inactivation by SspA
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-
?
elastin + H2O
elastin proteolytically cleaved into peptide fragments
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insoluble substrate
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-
?
HMW-kininogen + H2O
HMW-kininogen proteolytically cleaved into peptide fragments
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limited proteolysis
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-
?
N-benzyloxycarbonyl-Phe-Leu-Glu-NH-p-nitroanilide + H2O
N-benzyloxycarbonyl-Phe-Leu-Glu + p-nitroaniline
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-
-
-
?
Z-Phe-Leu-Glu-p-nitroanilide + H2O
Z-Phe-Leu-Glu + p-nitroaniline
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-
-
?
?
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substrate for ScpA
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-
?
5-carboxyfluorescein-Lys-Lys-Ala-Ala-Glu-Ala-Ser-Lys-(QXL520)-OH + H2O
?
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substrate for ScpA
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-
?
alcohol dehydrogenase proteolytically cleaved into peptide fragments
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-
-
-
?
alcohol dehydrogenase + H2O
alcohol dehydrogenase proteolytically cleaved into peptide fragments
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-
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
?
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substrate for SspB
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-
?
Bz-Pro-Phe-Arg + 4-nitroaniline
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chromogenic substrate
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-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
Bz-Pro-Phe-Arg + 4-nitroaniline
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chromogenic substrate
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-
?
casein proteolytically cleaved into peptide fragments
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-
-
-
?
casein + H2O
casein proteolytically cleaved into peptide fragments
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-
-
-
?
Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
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-
?
?
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the enzyme specifically cleaves the N-terminal domain of human CXCR2 between asparate-35 and alanine-36
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-
?
CXCR2 + H2O
?
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the enzyme specifically cleaves the N-terminal domain of human CXCR2 between asparate-35 and alanine-36
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-
?
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
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-
?
cystatin C + H2O
?
Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair function as protease inhibitor
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-
?
cystatin C + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
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-
?
cystatin C + H2O
?
Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair function as protease inhibitor
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-
?
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
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-
?
cystatin D + H2O
?
Ala10 bond hydrolyzed by staphopain A, truncation shown to impair inhibition of additional targets
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-
?
cystatin D + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
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-
?
cystatin D + H2O
?
Ala10 bond hydrolyzed by staphopain A, truncation shown to impair inhibition of additional targets
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-
?
?
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rather slow degradation through Sscp A
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-
?
fibrinogen A alpha chain + H2O
?
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Sscp B cleaves the fibrinogen A alpha-chain at the C-terminal region very efficiently
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-
?
?
the enzyme has galectin-3-processing capacity
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-
?
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
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-
?
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
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-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity
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-
?
hemoglobin proteolytically cleaved into peptide fragments
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-
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?
hemoglobin + H2O
hemoglobin proteolytically cleaved into peptide fragments
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-
-
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?
kinin + ?
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activation of human protein by SspA, kinin generation is responsible for infection associated pain and endema
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-
?
N-Suc-Gly-Phe-Gly + p-nitroaniline
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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
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-
?
N-Suc-Gly-Phe-Gly-p-nitroanilide + H2O
N-Suc-Gly-Phe-Gly + p-nitroaniline
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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
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-
?
peptide proteolytically cleaved into fragments or single amino acids
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-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
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broad specificity
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-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
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-
-
-
?
protein proteolytically cleaved into peptide fragments
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-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
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broad specificity
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-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
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enzyme may play a role in growth regulation
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-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
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-
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?
?
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staphopains A and B are cysteine proteases, staphopain shows no activity with casein
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-
?
additional information
?
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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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-
?
additional information
?
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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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-
?
additional information
?
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staphopain A does not cleave human CXCR1
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?
additional information
?
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staphopain A does not cleave human CXCR1
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?
additional information
?
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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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-
?
additional information
?
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inhibitory interactions among staphopains and staphostatins determined, staphopain A of Staphylococcus epidermidis purified and used for interaction analysis
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?
additional information
?
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inhibitory interactions among staphopains and staphostatins determined and used for interaction analysis
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?