3.4.22.10: streptopain
This is an abbreviated version!
For detailed information about streptopain, go to the full flat file.
Word Map on EC 3.4.22.10
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3.4.22.10
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speb
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streptococci
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glomerulonephritis
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zymogen
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fasciitis
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superantigens
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streptolysin
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nephritogenic
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streptokinase
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poststreptococcal
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scarlet
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apsgn
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shock-like
- 3.4.22.10
- speb
- streptococci
- glomerulonephritis
- zymogen
- fasciitis
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superantigens
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streptolysin
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nephritogenic
- streptokinase
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poststreptococcal
-
scarlet
-
apsgn
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shock-like
Reaction
preferential cleavage with hydrophobic residues at P2, P1 and P1' =
Synonyms
EC 3.4.4.18, IdeS, IgG-degrading enzyme of Streptococcus pyogenes, interleukin-1beta convertase, More, proteinase, streptococcal, pyrogenic exotoxin B, SCP, SpcCEP, Spe B, SPE B protease, SPE B/SCP, SpeB, SPP, Steptococcus proteinase, streptococcal cysteine protease, Streptococcal cysteine proteinase, streptococcal erythrogenic toxin B, streptococcal proteinase, streptococcal pyogenic exotoxin B, streptococcal pyrogenic exotoxin B, streptococcal pyrogenic exotoxin B/cysteine protease, Streptococcus peptidase A, Streptococcus protease, streptopain
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3.4.22.10 streptopainAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.22.10 - streptopain
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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
C5a peptidase + H2O
?
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cleavage sites are APA-K, AVI-D, SGTS, and C-terminally
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-
?
complement factor C3b + H2O
?
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cleavage sites are RTL-D, NHK-L, LAR-S, and VEL-I
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-
?
Fba + H2O
?
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a cell surface factor H- and factor H-like protein 1-binding protein of epithelial human cells, the enzyme inhibits complement regulatory protein factor H- and factor H-like protein 1 binding by proteolysis of the Fba protein, overview
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-
?
Fibrinogen + H2O
?
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cleavage sites are C-terminally in Aalpha chains
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-
?
Human fibrinogen + H2O
?
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release and processing, the enzyme abolishes the binding of Streptococcus pyogenes to full-length or 30 kDa fragment of human fibrinogen Fn, kinetics overview
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-
?
immunoglobulin G + H2O
?
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cleavage site is LLG-G in gamma-chain
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-
?
mouse CXCL-2 + H2O
?
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the cleavage site is between lysine residues K65 and K66
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-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
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cleavage site is YVH-D
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-
?
SpeBz + H2O
mature SpeB + ?
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auto-cleavage sites are AIK-A, KVN-L, QIK-E, TYA-G, and EIK-Q
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-
?
urokinase receptor + H2O
?
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cleavage site is close to the GPI anchor
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?
human CXCL-1 + H2O
?
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the cleavage site is between lysine residues K60 and K61
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?
human CXCL-1 + H2O
?
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the cleavage site is between lysine residues K60 and K61
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-
?
human CXCL-2 + H2O
?
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the cleavage site is between lysine residues K60 and K61
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-
?
human CXCL-2 + H2O
?
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the cleavage site is between lysine residues K60 and K61
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-
?
IgG + H2O
?
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the ability to cleave off the Fc part of antigen-bound IgG contributes to the escape of group A streptococci from opsonophygocytosis while not interfering with the formation of a host-like coat by unspecific IgG binding
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?
IgG + H2O
?
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the ability to cleave off the Fc part of antigen-bound IgG contributes to the escape of group A streptococci from opsonophygocytosis while not interfering with the formation of a host-like coat by unspecific IgG binding
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?
mouse CXCL-1 + H2O
?
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the cleavage site is between lysine residues K65 and K66
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?
mouse CXCL-1 + H2O
?
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the cleavage site is between lysine residues K65 and K66
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-
?
properdin + H2O
?
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cleavage of properdin leads to inhibition of complement-mediated opsonophagocytosis and bacterial killing by neutrophils, alternative complement pathway overview
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-
?
protein F1 + H2O
?
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SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1, e.g. in human pharyngeal epithelial cells Detroit 562, while proteins H and M1 are protected by plasma proteins, overview
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?
additional information
?
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the enzyme activates a 66000 Da matrix metalloprotease produced by human endothelial cells, a process that may contribute to endothelial cell damage, tissue destruction, and hemodynamic derangement
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?
additional information
?
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by removal of M1 protein and protein H from the streptococcal surface the enzyme regulates the bacterial cell-cell interactions, and perhaps also interactions with epithelial cells. Through expression of streptopain the enzyme can modify the composition of the surface proteins in response to environmental conditions. Such a mechanism will facilitate the adaption of the bacterium to its host
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?
additional information
?
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the enzyme can enhance the invasion ability of group A streptococci in human respiratory epithelial cells
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?
additional information
?
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the expression of the enzyme contributes to soft tissue pathology, including necrosis, and is required for efficient systemic dissemination of the organism from the initial site of skin inoculation
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?
additional information
?
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release of biological active kinins from kininogens present in human plasma
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?
additional information
?
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the enzyme is an important virulence factor
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?
additional information
?
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the enzyme is secreted under conditions of starvation and may be involved in nutrient acquisition
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?
additional information
?
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thus, although IgG might by a substrate for SpeB under certain environmental conditions, it seems unlikely that SpeB is part of the first line of defense against specific antibodies. Even though SpeB might not be directly involved in the attenuation of the adaptive immune response, its proteolytic activity towards streptococcal surface proteins, including IgG-binding proteins and the streptococcal C5a peptidase, could certainly be important for the modulation of the complement system
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?
additional information
?
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streptopain shows strepadhesin activity, independent of protease activity, mediated by a cell surface adhesin and controlled by the multiple gene regulator Mga
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?
additional information
?
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the enzyme can induce apoptosis in A549 cells, the induction of apoptosis in cells requires the protease activity and the propper enzyme size of 28 kDa, cell binding activity of processed and unprocessed wild-type and mutant enzymes, the induction can be prevented by inhibition of caspase-8, induction cascade, overview
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?
additional information
?
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the enzyme inactivates the metabolic activity of polymorphonuclear cells, the enzyme causes mitochondria damage to polymorphonuclear cells preventing phagocytosis of group A Streptococcus, it is essential for bacterial survival in blood, mechanism, overview
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?
additional information
?
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the enzyme is a virulence factor of Streptococcus pyogenes inducing the release of histamine in mast cells, basophils, and mononuclear cells, and increasing capillary permeability and histamine release in skin of guinea pigs, the recombinant enzyme shows mitogenic activity with human T-cells
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?
additional information
?
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CXCL9 is quite resistant to hydrolysis by SpeB
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?
additional information
?
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incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37°C does not cause degradation of the protein
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?
additional information
?
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SpeB has no immunoglobulin-degrading activity in human plasma or blood
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?
additional information
?
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the enzyme can induce apoptosis in A549 cells, the induction of apoptosis in cells requires the protease activity and the propper enzyme size of 28 kDa, cell binding activity of processed and unprocessed wild-type and mutant enzymes, the induction can be prevented by inhibition of caspase-8, induction cascade, overview
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?
additional information
?
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incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37°C does not cause degradation of the protein
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?
additional information
?
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incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37°C does not cause degradation of the protein
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?
additional information
?
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the enzyme is not critical for the development of tissue necrosis, bacteremia and lethal infection in a murine model of human necrotizing fascilitis
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?
additional information
?
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critical virulence factor for invasive disease episode. Binds host cell integrins alphaVbeta3 and alphaIIbbeta3 through an RGD motif
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?
