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Information on EC 3.4.22.10 - streptopain
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3.4.22.10 streptopainSpecify your search results
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- 3.4.22.10
- speb
- streptococci
- glomerulonephritis
- zymogen
- fasciitis
-
superantigens
-
streptolysin
-
nephritogenic
- streptokinase
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poststreptococcal
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scarlet
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apsgn
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shock-like
The enzyme appears in viruses and cellular organisms
Synonyms
spe b, streptococcal pyrogenic exotoxin b, streptococcal proteinase, streptopain, streptococcal cysteine protease, pyrogenic exotoxin b, streptococcal cysteine proteinase, spe b/scp, streptococcal erythrogenic toxin b, igg-degrading enzyme of streptococcus pyogenes, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.4.4.18
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formerly
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proteinase, streptococcal
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-
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SCP
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SpcCEP
Spe B
SPE B protease
SpeB
SPP
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Steptococcus proteinase
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streptococcal cysteine protease
Streptococcal cysteine proteinase
streptococcal pyogenic exotoxin B
streptococcal pyrogenic exotoxin B
Streptococcus peptidase A
Streptococcus protease
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streptopain
additional information
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the enzyme belongs to the peptidase family C10
Spe B
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SpeB
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Streptococcal cysteine proteinase
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streptococcal pyrogenic exotoxin B
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Streptococcus peptidase A
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential cleavage with hydrophobic residues at P2, P1 and P1'
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preferential cleavage with hydrophobic residues at P2, P1 and P1'
catalytic residue Cys192
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preferential cleavage with hydrophobic residues at P2, P1 and P1'
the catalytic residue is His195 forming an ion pair with the single Cys47 residue
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY
9025-51-8
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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
benzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly + p-nitrophenol
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-
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?
C5a peptidase + H2O
?
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cleavage sites are APA-K, AVI-D, SGTS, and C-terminally
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?
cinnamoyl-Gly-p-nitrophenyl ester + H2O
cinnamoyl-Gly + 4-nitrophenol
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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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?
human interleukin 1beta precursor + H2O
human interleukin 1beta + human interleukin 1beta signal peptide
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?
IgD + H2O
?
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degradation of the carboxy-terminal part of the heavy chain
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?
IgE + H2O
?
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degradation of the carboxy-terminal part of the heavy chain
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?
IgG + H2O
Fab fragment + Gc fragments
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the enzyme cleaves IgG in the flexible hinge region of the IgG heavy chain, generating two Fab fragments and Fc fragment. SpeB cleaves the heavy chain at a defined site between glycine residues 236 and 237
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?
immunoglobulin G + H2O
?
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cleavage site is LLG-G in gamma-chain
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?
immunoglobulin G + H2O
F(ab')2 + 1/2Fc
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non-immune binding of IgG to the bacterial surface is followed by the proteolytic cleavage of the antibody by the IgG-endopeptidase IdeS. IdeS generated 1/2Fc fragments do not compete efficiently with intact IgG in binding to the bacterial surface and rapid dissociation of 1/2Fc allows binding of new IgG. A correlated binding and proteolytic cleavage of IgG increases the probability that the bacteria can resist specific IgG, despite the presence of a large excess of non-specific IgG in the circulation. As a consequence of IdeS activity, circulating 1/2Fc fragments are generated. These 1/2Fc fragments are shown to be biological active by acting as priming agents for polymorphonuclear leucocytes
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?
immunoglobulin G + H2O
F(ab')2 fragment + 1/2 Fc fragments
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IdeS cleaves IgG by hydrolyzing the peptide bond between two glycine residues in the hinge region of IgG, generating one F(ab')2 fragment and two 1/2 Fc fragments
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?
insulin + H2O
?
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reduced carboxymethylated phenylalanine chain, one of the most rapidly hydrolyzed Phe-Tyr linkages is in the Phe-Phe-Tyr sequence
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?
insulin beta chain + H2O
?
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reduced and carboxylated substrate, cleavage of the linkage Phe25-Tyr26
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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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?
N-benzoyl-Gly-p-nitrophenyl ester + H2O
N-benzoyl-Gly + 4-nitrophenol
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?
N-benzyloxycarbonyl-Ala-p-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Ala + 4-nitrophenol
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?
N-benzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly + 4-nitrophenol
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?
Nalpha-benzyloxycarbonyl-Lys-phenyl ester + H2O
Nalpha-benzyloxycarbonyl-Lys + phenol
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?
Nalpha-benzyloxycarbonyl-Nepsilon-t-butyloxycarbonyl-Lys-Phe + H2O
?
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?
Nalpha-benzyloxycarbonyl-Nepsilon-tosyl-Lys-p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-Nepsilon-tosyl-Lys + p-nitrophenol
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?
Nepsilon-benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
Nepsilon-benzyloxycarbonyl-Lys + 4-nitrophenol
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?
p-nitrobenzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
p-nitrobenzyloxycarbonyl-Gly + 4-nitrophenol
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?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
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cleavage site is YVH-D
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?
proSPE B C47S + H2O
?
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the proSPE B C47S mutant is also be used as the substrate for activity assay because it does not exhibit any enzyme activity and exists as a 42 kDa zymogen
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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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?
streptococcal mitogenic exotoxin SmeZ + H2O
?
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cleaves between glutamate and glycine residues
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?
streptococcal mitogenic exotoxin SpeG + H2O
?
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partial degradation, SpeB cleaves between glutamate and glycine residues
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?
t-butyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
t-butyloxycarbonyl-Gly + 4-nitrophenol
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?
tert-butyloxycarbonyl-Ala-p-nitrophenyl ester + H2O
tert-butyloxycarbonyl-Ala + 4-nitrophenol
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?
urokinase receptor + H2O
?
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cleavage site is close to the GPI anchor
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?
acetyl-Ala-Ile-Arg-7-amino-4-methylcoumarin + H2O
?
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?
benzyloxycarbonyl-Val-Arg-4-methylcoumarinyl-7-amide + H2O
?
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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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?
Fba + H2O
?
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a cell surface factor H- and factor H-like protein 1-binding protein of epithelial human cells
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?
Fibrinogen + H2O
?
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cleavage sites are C-terminally in Aalpha chains
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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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?
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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?
IgA + H2O
?
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degradation of the carboxy-terminal part of the heavy chain
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?
IgA + H2O
?
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efficiently cleaved under reducing conditions but not under nonreducing conditions
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?
IgG + H2O
?
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efficiently cleaved under reducing conditions but not under nonreducing conditions
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?
IgG + H2O
?
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cleaves off the Fc part of antigen-bound IgG, the cleavage of IgG is not species restricted
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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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cleaves off the Fc part of antigen-bound IgG, the cleavage of IgG is not species restricted
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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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?
IgM + H2O
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degradation of the carboxy-terminal part of the heavy chain
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?
IgM + H2O
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efficiently cleaved under reducing conditions but not under nonreducing conditions
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?
interleukin-1beta precursor + H2O
interleukin-1beta + interleukin-1beta propeptide
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?
interleukin-1beta precursor + H2O
interleukin-1beta + interleukin-1beta propeptide
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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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an unprotonated imidazole ring and the protonated form of the single sulfhydryl group are essential for activity
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?
additional information
?
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the enzyme also at low concentrations efficiently removes M1 protein and protein H from the streptococcal surface
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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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cleavage site specificity, overview, the enzyme prefers cleavage of Phe-Tyr bonds, the enzyme shows poor activity with trypsin substrates fibrin, casein, and gelatin from human and rabbit
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?
additional information
?
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Spi and the Spe B pro-peptide both bind to mature Spe B, but are no substrates
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?
additional information
?
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the enzyme performs autolytic activity and also cleaves the inactive mutant C192S
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?
additional information
?
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the enzyme performs autolytic processing to the mature protein, interaction overview
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?
additional information
?
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does not cleave streptococcal mitogenic exotoxins SpeA and SpeJ
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?
additional information
?
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the three-dimensional structure and backbone dynamics of the 28 kDa mature SPE B (mSPE B) is determined: Interactions between the C-terminal loop and the active site residues in mSPE B are observed. The structural differences between mSPE B and zymogen proSPE B are the conformation of the C-terminal loop and the orientation of the catalytic His-195 residue. Dynamics analysis of mSPEB and the mSPEB/inhibitor complexes show that the catalytic and C-terminal loops are the most flexible regions, suggesting that the flexible C-terminal loop of SPE B may play an important role in controlling the substrate binding, resulting in its broad substrate specificity
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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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streptopain can cleave a wide range of human proteins, including immunoglobulins, the complement activation system, chemokines, and structural proteins
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?
additional information
?
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streptopain can cleave a wide range of human proteins, including immunoglobulins, the complement activation system, chemokines, and structural proteins
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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 performs autolytic activity and also cleaves the inactive mutant C192S
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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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Spi and the Spe B pro-peptide both bind to mature Spe B, but are no substrates
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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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?
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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
?
-
cleavage sites are APA-K, AVI-D, SGTS, and C-terminally
-
-
?
complement factor C3b + H2O
?
-
cleavage sites are RTL-D, NHK-L, LAR-S, and VEL-I
-
-
?
Fba + H2O
?
-
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
-
-
?
Fibrinogen + H2O
?
-
cleavage sites are C-terminally in Aalpha chains
-
-
?
Human fibrinogen + H2O
?
-
release and processing, the enzyme abolishes the binding of Streptococcus pyogenes to full-length or 30 kDa fragment of human fibrinogen Fn, kinetics overview
-
-
?