Information on EC 3.4.22.10 - streptopain

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The expected taxonomic range for this enzyme is: Streptococcus

EC NUMBER
COMMENTARY
3.4.22.10
-
RECOMMENDED NAME
GeneOntology No.
streptopain
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
preferential cleavage with hydrophobic residues at P2, P1 and P1'
show the reaction diagram
-
-
-
-
preferential cleavage with hydrophobic residues at P2, P1 and P1'
show the reaction diagram
catalytic residue Cys192
-
preferential cleavage with hydrophobic residues at P2, P1 and P1'
show the reaction diagram
the catalytic residue is His195 forming an ion pair with the single Cys47 residue
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EC 3.4.4.18
-
-
formerly
-
IgG-degrading enzyme of Streptococcus pyogenes
-
-
proteinase, streptococcal
-
-
-
-
pyrogenic exotoxin B
-
-
SCP
-
-
-
-
SpcCEP
Streptococcus pyogenes H292
-
-
-
Spe B
-
-
-
-
Spe B
Streptococcus pyogenes A-20
-
-
-
SPE B protease
Streptococcus pyogenes A-20, Streptococcus pyogenes B220
-
-
-
SpeB
Streptococcus pyogenes Alab49, Streptococcus pyogenes AP1, Streptococcus pyogenes B220
-
-
-
SpeB
P0C0J1
-
-
SpeB
Streptococcus sp. MGAS315, Streptococcus sp. RGAS053, Streptococcus sp. strainT1BRB
-
-
-
SPP
-
-
-
-
Steptococcus proteinase
-
-
-
-
streptococcal cysteine protease
-
-
streptococcal cysteine protease
Streptococcus pyogenes B220
-
-
-
Streptococcal cysteine proteinase
-
-
-
-
Streptococcal cysteine proteinase
-
-
streptococcal erythrogenic toxin B
-
-
streptococcal proteinase
-
-
streptococcal pyogenic exotoxin B
-
-
streptococcal pyogenic exotoxin B
Streptococcus pyogenes Alab49, Streptococcus pyogenes AP1
-
-
-
streptococcal pyrogenic exotoxin B
-
-
streptococcal pyrogenic exotoxin B
P0C0J0
-
streptococcal pyrogenic exotoxin B
P0C0J1
-
streptococcal pyrogenic exotoxin B
Streptococcus pyogenes A-20
-
-
-
streptococcal pyrogenic exotoxin B
P0C0J1
-
-
streptococcal pyrogenic exotoxin B
-
-
streptococcal pyrogenic exotoxin B/cysteine protease
-
-
Streptococcus peptidase A
-
-
-
-
Streptococcus peptidase A
-
-
Streptococcus protease
-
-
-
-
interleukin-1beta convertase
-
-
additional information
-
the enzyme belongs to the peptidase family C10
CAS REGISTRY NUMBER
COMMENTARY
9025-51-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; serotype M1
-
-
Manually annotated by BRENDA team
precursor; strain HSC5
UniProt
Manually annotated by BRENDA team
several AP strains
-
-
Manually annotated by BRENDA team
strain A-20
-
-
Manually annotated by BRENDA team
the enzyme is expressed in all strains
-
-
Manually annotated by BRENDA team
Streptococcus pyogenes A-20
strain A-20
-
-
Manually annotated by BRENDA team
Streptococcus pyogenes AP1
serotype M1
-
-
Manually annotated by BRENDA team
Streptococcus pyogenes B220
strain B220
-
-
Manually annotated by BRENDA team
Streptococcus pyogenes H292
-
-
-
Manually annotated by BRENDA team
precursor; strain HSC5
UniProt
Manually annotated by BRENDA team
group A
-
-
Manually annotated by BRENDA team
hemolytic
-
-
Manually annotated by BRENDA team
serotype M1; serotype M3
-
-
Manually annotated by BRENDA team
strain T10BW
-
-
Manually annotated by BRENDA team
strainT1BRB
-
-
Manually annotated by BRENDA team
Streptococcus sp. MGAS315
serotype M3
-
-
Manually annotated by BRENDA team
Streptococcus sp. RGAS053
serotype M1
-
-
Manually annotated by BRENDA team
Streptococcus sp. strainT1BRB
strainT1BRB
-
-
Manually annotated by BRENDA team
Streptococcus sp. T10BW
strain T10BW
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
addition of SpeB to human plasma increases plasma-mediated bacterial killing and prolonged coagulation time through the intrinsic pathway of coagulation. This effect is independent of the enzymatic activity of SpeB and is mediated by a noncovalent medium-affinity binding and modification of alpha-1 antitrypsin
physiological function
-
in infected mice, SpyCEP expression by Streptococcus pyogenes hinders bacterial clearance from muscle, and enhances bacterial spread, associated with cleavage of CXCL1. SpyCEP is necessary and sufficient for bacterial dissemination within soft tissues. SpyCEP enhances Streptococcus pyogenes dissemination to lower respiratory tract from nasopharynx
physiological function
-
the streptococcal regulator of virulence control of SpeB production is a mechanism to regulate biofilm dispersal and provides a mechanism by which mild infection can transition to severe disease
physiological function
Streptococcus pyogenes Alab49, Streptococcus pyogenes AP1
-
addition of SpeB to human plasma increases plasma-mediated bacterial killing and prolonged coagulation time through the intrinsic pathway of coagulation. This effect is independent of the enzymatic activity of SpeB and is mediated by a noncovalent medium-affinity binding and modification of alpha-1 antitrypsin
-
physiological function
Streptococcus pyogenes H292
-
in infected mice, SpyCEP expression by Streptococcus pyogenes hinders bacterial clearance from muscle, and enhances bacterial spread, associated with cleavage of CXCL1. SpyCEP is necessary and sufficient for bacterial dissemination within soft tissues. SpyCEP enhances Streptococcus pyogenes dissemination to lower respiratory tract from nasopharynx
-
physiological function
Streptococcus sp. MGAS315, Streptococcus sp. RGAS053
-
the streptococcal regulator of virulence control of SpeB production is a mechanism to regulate biofilm dispersal and provides a mechanism by which mild infection can transition to severe disease
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-aminobenzoyl-Ala-Ala-Ile-Lys-Ala-Gly-Ala-Arg + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes B220
-
-
-
-
?
3-aminobenzoyl-Ala-Glu-Ile-Lys-Gln-Pro-Val-Val + H2O
?
show the reaction diagram
-
-
-
-
?
3-aminobenzoyl-Asp-Lys-Val-Asn-Leu-Gly-Gly-Glu + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes B220
-
-
-
-
?
3-aminobenzoyl-Glu-Gln-Ile-Lys-Glu-Asn-Lys-Lys + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes B220
-
-
-
-
?
3-aminobenzoyl-Thr-Thr-Thr-Ala-Gly-Thr-Ala-Glu + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes B220
-
-
-
-
?
alpha1-antitrypsin + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Glu-p-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-p-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly + p-nitrophenol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Nle-p-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Nle-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Val-Arg-4-methylcoumarinyl-7-amide hydrochloride + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes B220
-
-
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes B220
-
-
-
-
?
C5a peptidase + H2O
?
show the reaction diagram
-
cleavage sites are APA-K, AVI-D, SGTS, and C-terminally
-
-
?
casein + H2O
?
show the reaction diagram
P0C0J1
-
-
-
?
casein + H2O
?
show the reaction diagram
-
bovine
-
-
?
casein + H2O
?
show the reaction diagram
P0C0J1
-
-
-
?
cinnamoyl-Gly-p-nitrophenyl ester + H2O
cinnamoyl-Gly + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
complement component C3 + H2O
?
show the reaction diagram
-
-
-
-
?
complement factor C3b + H2O
?
show the reaction diagram
-
cleavage sites are RTL-D, NHK-L, LAR-S, and VEL-I
-
-
?
D-Ile-Pro-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
decorin + H2O
?
show the reaction diagram
-
-
-
-
?
EndoS + H2O
?
show the reaction diagram
-
cleavage site is VML-K
-
-
?
Fba + H2O
?
show the reaction diagram
-
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, a cell surface factor H- and factor H-like protein 1-binding protein of epithelial human cells
-
-
?
Fba protein + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
human fibrinogen
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
cleavage sites are C-terminally in Aalpha chains
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
H-kininogen + H2O
biologically active kinins
show the reaction diagram
-
-
-
?
H-kininogen + H2O
?
show the reaction diagram
-
cleavage sites are LMK-R and PFR-S
-
-
?
human CXCL-1 + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes H292
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-2 + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes H292
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-6 + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes H292
-
-
-
-
?
human CXCL-8 + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes H292
-
-
-
-
?
human CXCL10 + H2O
?
show the reaction diagram
-
-
-
-
?
Human fibrinogen + H2O
?
show the reaction diagram
-
processing, release and processing, the enzyme abolishes the binding of Streptococcus pyogenes to full-length or 30 kDa fragment of human fibrinogen Fn, kinetics overview
-
-
?
human interleukin 1beta precursor + H2O
human interleukin 1beta + fragment
show the reaction diagram
-
-
-
-
?
IgA + H2O
?
show the reaction diagram
-
degradation of the carboxy-terminal part of the heavy chain
-
?
IgD + H2O
?
show the reaction diagram
-
degradation of the carboxy-terminal part of the heavy chain
-
?
IgE + H2O
?
show the reaction diagram
-
degradation of the carboxy-terminal part of the heavy chain
-
?
IgG + H2O
?
show the reaction diagram
-
cleaves off the Fc part of antigen-bound IgG, the cleavage of IgG is not species restricted, 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
-
?
IgG + H2O
?
show the reaction diagram
Streptococcus sp. strainT1BRB
-
cleaves off the Fc part of antigen-bound IgG, the cleavage of IgG is not species restricted, 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
-
?
IgG + H2O
Fab fragment + Gc fragments
show the reaction diagram
-
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
-
?
IgM + H2O
?
show the reaction diagram
-
degradation of the carboxy-terminal part of the heavy chain
-
?
immunoglobulin A + H2O
?
show the reaction diagram
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin D + H2O
?
show the reaction diagram
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin E + H2O
?
show the reaction diagram
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin G + H2O
?
show the reaction diagram
-
cleavage site is LLG-G in gamma-chain
-
-
?
immunoglobulin G + H2O
F(ab')2 + 1/2Fc
show the reaction diagram
-
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
-
-
?
immunoglobulin G + H2O
F(ab')2 fragment + 1/2 Fc fragments
show the reaction diagram
-
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
-
-
?
immunoglobulin M + H2O
?
show the reaction diagram
-
cleavage sites are the heavy chains
-
-
?
insulin + H2O
?
show the reaction diagram
-
reduced carboxymethylated phenylalanine chain, one of the most rapidly hydrolyzed Phe-Tyr linkages is in the Phe-Phe-Tyr sequence
-
-
?
insulin beta chain + H2O
?
show the reaction diagram
-
reduced and carboxylated substrate, cleavage of the linkage Phe25-Tyr26
-
-
?
interleukin-1beta precursor + H2O
interleukin -1beta + ?
show the reaction diagram
Streptococcus sp., Streptococcus sp. T10BW
-
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
mouse CXCL-1 + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes H292
-
the cleavage site is between lysine residues K65 and K66
-
-
?
mouse CXCL-2 + H2O
?
show the reaction diagram
-
the cleavage site is between lysine residues K65 and K66
-
-
?
N-benzoyl-Gly-p-nitrophenyl ester + H2O
N-benzoyl-Gly + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Ala-p-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Ala + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly + 4-nitrophenol
show the reaction diagram
-
-
-
-
-
N-benzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Lys-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Nepsilon-t-butyloxycarbonyl-Lys-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Nepsilon-tosyl-Lys-p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-Nepsilon-tosyl-Lys + p-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Phe-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Phe-Tyr + H2O
?
show the reaction diagram
-
-
-
-
?
Nepsilon-benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
Nepsilon-benzyloxycarbonyl-Lys + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
p-nitrobenzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
p-nitrobenzyloxycarbonyl-Gly + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-benzyloxycarbonyl-L-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
cleavage site is YVH-D
-
-
?
properdin + H2O
?
show the reaction diagram
-
-
-
-
?
properdin + H2O
?
show the reaction diagram
-
cleavage of properdin leads to inhibition of complement-mediated opsonophagocytosis and bacterial killing by neutrophils, alternative complement pathway overview
-
-
?
proSPE B C47S + H2O
?
show the reaction diagram
-
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
-
-
?
proSpeB + H2O
SpeB + ?
show the reaction diagram
P0C0J1
autoactivation
-
-
?
protein F1 + H2O
?
show the reaction diagram
-
-
-
-
?
protein F1 + H2O
?
show the reaction diagram
-
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, cell-wall-anchored protein F1
-
-
?
protein H + H2O
?
show the reaction diagram
-
-
-
-
?
resorufin-labeled casein + H2O
?
show the reaction diagram
-
-
-
-
?
Sda1 + H2O
?
show the reaction diagram
-
-
-
-
?
Slr + H2O
?
show the reaction diagram
-
-
-
-
?
SmeZ + H2O
?
show the reaction diagram
-
-
-
-
?
SpeBz + H2O
mature SpeB + ?
show the reaction diagram
-
auto-cleavage sites are AIK-A, KVN-L, QIK-E, TYA-G, and EIK-Q
-
-
?
streptococcal mitogenic exotoxin SmeZ + H2O
?
show the reaction diagram
-
cleaves between glutamate and glycine residues
-
-
?
streptococcal mitogenic exotoxin SpeG + H2O
?
show the reaction diagram
-
partial degradation, SpeB cleaves between glutamate and glycine residues
-
-
?
streptokinase + H2O
?
show the reaction diagram
-
-
-
-
?
streptolysin O + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
t-butyloxycarbonyl-Gly + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Ala-p-nitrophenyl ester + H2O
tert-butyloxycarbonyl-Ala + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
urokinase receptor + H2O
?
show the reaction diagram
-
cleavage site is close to the GPI anchor
-
-
?
Vitronectin + H2O
?
show the reaction diagram
-
-
-
-
?
M protein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
an unprotonated imidazole ring and the protonated form of the single sulfhydryl group are essential for activity, the enzyme also at low concentrations efficiently removes M1 protein and protein H from the streptococcal surface
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme can enhance the invasion ability of group A streptococci in human respiratory epithelial cells
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
release of biological active kinins from kininogens present in human plasma
-
-
-
additional information
?
-
-
the enzyme is an important virulence factor
-
-
-
additional information
?
-
-
the enzyme is not critical for the development of tissue necrosis, bacteremia and lethal infection in a murine model of human necrotizing fascilitis
-
-
-
additional information
?
-
-
critical virulence factor for invasive disease episode. Binds host cell integrins alphaVbeta3 and alphaIIbbeta3 through an RGD motif
-
-
-
additional information
?
-
-
the enzyme is secreted under conditions of starvation and may be involved in nutrient acquisition
-
-
-
additional information
?
-
-
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
-
?
additional information
?
-
-
streptopain shows strepadhesin activity, independent of protease activity, mediated by a cell surface adhesin and controlled by the multiple gene regulator Mga
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
Spi and the Spe B pro-peptide both bind to mature Spe B, but are no substrates
-
-
-
additional information
?
-
-
the enzyme performs autolytic activity and also cleaves the inactive mutant C192S
-
-
-
additional information
?
-
-
the enzyme performs autolytic processing to the mature protein, interaction overview
-
-
-
additional information
?
-
-
does not cleave streptococcal mitogenic exotoxins SpeA and SpeJ
-
-
-
additional information
?
-
-
SPE B is able to autoactivate
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
CXCL9 is quite resistant to hydrolysis by SpeB
-
-
-
additional information
?
-
-
incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37C does not cause degradation of the protein
-
-
-
additional information
?
-
Streptococcus pyogenes A-20
-
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, the enzyme performs autolytic activity and also cleaves the inactive mutant C192S
-
-
-
additional information
?
-
Streptococcus pyogenes B220
-
Spi and the Spe B pro-peptide both bind to mature Spe B, but are no substrates
-
-
-
additional information
?
-
Streptococcus pyogenes Alab49, Streptococcus pyogenes AP1
-
incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37C does not cause degradation of the protein
-
-
-
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
alpha1-antitrypsin + H2O
?
show the reaction diagram
-
-
-
-
?
C5a peptidase + H2O
?
show the reaction diagram
-
cleavage sites are APA-K, AVI-D, SGTS, and C-terminally
-
-
?
complement factor C3b + H2O
?
show the reaction diagram
-
cleavage sites are RTL-D, NHK-L, LAR-S, and VEL-I
-
-
?
decorin + H2O
?
show the reaction diagram
-
-
-
-
?
EndoS + H2O
?
show the reaction diagram
-
cleavage site is VML-K
-
-
?
Fba + H2O
?
show the reaction diagram
-
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
-
-
?
Fba protein + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
cleavage sites are C-terminally in Aalpha chains
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
H-kininogen + H2O
?
show the reaction diagram
-
cleavage sites are LMK-R and PFR-S
-
-
?
human CXCL-1 + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes H292
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-2 + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes H292
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-6 + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes H292
-
-
-
-
?
human CXCL-8 + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes H292
-
-
-
-
?
human CXCL10 + H2O
?
show the reaction diagram
-
-
-
-
?
Human fibrinogen + H2O
?
show the reaction diagram
-
release and processing, the enzyme abolishes the binding of Streptococcus pyogenes to full-length or 30 kDa fragment of human fibrinogen Fn, kinetics overview
-
-
?
IgG + H2O
?
show the reaction diagram
Streptococcus sp., Streptococcus sp. strainT1BRB
-
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
-
?
immunoglobulin A + H2O
?
show the reaction diagram
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin D + H2O
?
show the reaction diagram
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin E + H2O
?
show the reaction diagram
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin G + H2O
?
show the reaction diagram
-
cleavage site is LLG-G in gamma-chain
-
-
?
immunoglobulin M + H2O
?
show the reaction diagram
-
cleavage sites are the heavy chains
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
-
?
mouse CXCL-1 + H2O
?
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes H292
-
the cleavage site is between lysine residues K65 and K66
-
-
?
mouse CXCL-2 + H2O
?
show the reaction diagram
-
the cleavage site is between lysine residues K65 and K66
-
-
?
plasminogen + H2O
?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
cleavage site is YVH-D
-
-
?
properdin + H2O
?
show the reaction diagram
-
-
-
-
?
properdin + H2O
?
show the reaction diagram
-
cleavage of properdin leads to inhibition of complement-mediated opsonophagocytosis and bacterial killing by neutrophils, alternative complement pathway overview
-
-
?
protein F1 + H2O
?
show the reaction diagram
-
-
-
-
?
protein F1 + H2O
?
show the reaction diagram
-
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
-
-
?
protein H + H2O
?
show the reaction diagram
-
-
-
-
?
Sda1 + H2O
?
show the reaction diagram
-
-
-
-
?
Slr + H2O
?
show the reaction diagram
-
-
-
-
?
SmeZ + H2O
?
show the reaction diagram
-
-
-
-
?
SpeBz + H2O
mature SpeB + ?
show the reaction diagram
-
auto-cleavage sites are AIK-A, KVN-L, QIK-E, TYA-G, and EIK-Q
-
-
?
streptokinase + H2O
?
show the reaction diagram
-
-
-
-
?
streptolysin O + H2O
?
show the reaction diagram
-
-
-
-
?
urokinase receptor + H2O
?
show the reaction diagram
-
cleavage site is close to the GPI anchor
-
-
?
Vitronectin + H2O
?
show the reaction diagram
-
-
-
-
?
M protein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme can enhance the invasion ability of group A streptococci in human respiratory epithelial cells
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
release of biological active kinins from kininogens present in human plasma
-
-
-
additional information
?
-
-
the enzyme is an important virulence factor
-
-
-
additional information
?
-
-
the enzyme is not critical for the development of tissue necrosis, bacteremia and lethal infection in a murine model of human necrotizing fascilitis
-
-
-
additional information
?
-
-
critical virulence factor for invasive disease episode. Binds host cell integrins alphaVbeta3 and alphaIIbbeta3 through an RGD motif
-
-
-
additional information
?
-
-
the enzyme is secreted under conditions of starvation and may be involved in nutrient acquisition
-
-
-
additional information
?
-
-
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
-
?
additional information
?
-
-
streptopain shows strepadhesin activity, independent of protease activity, mediated by a cell surface adhesin and controlled by the multiple gene regulator Mga
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
CXCL9 is quite resistant to hydrolysis by SpeB
-
-
-
additional information
?
-
-
incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37C does not cause degradation of the protein
-
-
-
additional information
?
-
Streptococcus pyogenes A-20
-
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
-
-
-
additional information
?
-
Streptococcus pyogenes Alab49, Streptococcus pyogenes AP1
-
incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37C does not cause degradation of the protein
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
bisulfite
-
reduction is essential for catalytic activity
cyanide
-
reduction is essential for catalytic activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(S)-1-azido-2-tosylamino-hexane
-
moderate inhibitor of IdeS
(S)-1-azido-3-methyl-2-tosylamino-butane
-
moderate inhibitor of IdeS
(S)-1-azido-3-phenyl-2-tosylamino-propane
-
moderate inhibitor of IdeS
(S)-3-tosylamino-1-heptanal
-
strong inhibitory activity
(S)-3-tosylamino-heptane-1-nitrile
-
the compound shows some inhibition of IdeS
(S)-4-methyl-3-tosylamino-1-pentanal
-
strong inhibitory activity
(S)-4-phenyl-3-tosylamino-1-butanal
-
strong inhibitory activity
(S)-7-tert-butoxycarbonylamino-3-tosylamino-1-heptanal
-
strong inhibitory activity
1,3-Dibromoacetone
-
rapid and complete loss of activity
acetonitrile
-
mixed type
benzyloxycarbonyl-Ala-Ala-CHN2
-
-
benzyloxycarbonyl-Ala-Ala-Pro-CHN2
-
-
benzyloxycarbonyl-Ala-Phe-Ala-CHN2
-
-
benzyloxycarbonyl-Asn-Val-Gly-CHN2
-
inhibition of protease activity, no influence on the superantigenic properties of the enzyme
Benzyloxycarbonyl-Gly-Phe
-
competitive against benzyloxycarbonyl-Phe-Tyr
benzyloxycarbonyl-Leu-Val-Gly-CHN2
-
inhibits kininogen degradation
Benzyloxycarbonyl-Phe-Ala-CHN2
-
-
benzyloxycarbonyl-Phe-Gly-CHN2
-
-
benzyloxycarbonyl-Phe-Gly-Phe-CHN2
-
-
dimethyl sulfoxide
-
competitive
Dinitrofluorobenzene
-
-
-
E-64
-
i.e. L-trans-epoxysuccinyl-leucylamido(4-guanidino)butane, irreversible inhibition
E64
-
i.e. trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
Gly-Phe-CHN2
-
-
HgCl2
-
prevents the conversion to the mature 28 kDa form
iodoacetate
-
irreversible inhibitor
iodoacetic acid
-
-
L-trans-epoxysuccinyl-leucylamido(4-guanidino)butane
-
-
N-[N-(L-3-transcarboxyirane-2-carbonyl)-L-leucyl]agmatine
P0C0J1
-
Nalpha-benzyloxycarbonyl-Phe-Phe
-
strong inhibition of hydrolysis of Nalpha-benzyloxycarbonyl-Phe-Tyr
Sodium tetrathionate
-
-
Spe B pro-peptide
-
specific inhibition of the mature enzyme, secondary structure and SpeB binding analysis, inhibition modeling and mechanism, overview
-
Spi
-
specific enzyme pro-peptide analogue inhibitor, purification from Streptococcus pyogenes, secondary structure and SpeB binding analysis, inhibition modeling and mechanism, overview
-
tosyl-L-lysine chloromethyl ketone
-
irreversible inhibitor
tosyl-L-phenylalanine chloromethyl ketone
-
irreversible inhibitor
Tosyl-norleucine-Phe
-
competitive against benzyloxycarbonyl-norleucine-Phe
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E64, inhibits the capillary permeability increasing effect of the enzyme
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E64, complete inhibition at 0.016 mM
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E64
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
-
Z-LVG-CHN2
-
irreversible inhibitor
methyliodine
-
-
-
additional information
-
IdeS is not inhibited by E-64, (S)-3-phenyl-2-tosylamino-1-propanol, (S)-2-tosylamino-1-hexanol, (S)-3-methyl-2-tosylamino-1-butanol, (S)-6-tert-butoxycarbonylamino-2-tosylamino-1-hexanol, (S)-6-amino-2-tosylamino-1-hexanol trifluoroacetic acid, (S)-3-phenyl-2-tosylamino-propyl-1-toluenesulfonate, (S)-2-tosylamino-hexyl-1-toluenesulfonate, (S)-3-methyl-2-tosylamino-butyl-1-toluenesulfonate, and (S)-6-tert-butoxycarbonylamino-2-tosylamino-hexyl-1-toluenesulfonate
-
additional information
-
antibodies produced against the r28-kDa truncated form of the C192 mutant enzyme effectively inhibit digestion of casein or fibrinogen by cysteine protease wheras antibodies generated against the r40-kDA form of the mutant have no significant effect on proteolysis
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Reducing agent
-
once the enzyme is activated by a reducing agent, the presence of the activator is no longer necessary for the catalytic activity
-
thioethanol
-
reduction is essential for catalytic activity, once the enzyme is activated by the reducing agent, the presence of the activator is no longer necessary for catalytic activity
thioglycolic acid
-
reduction is essential for catalytic activity
dithiothreitol
-
reduction is essential for catalytic activity
additional information
-
incubation with human alveolar basal epithelial A549 cells induce enzyme expression
-
additional information
P0C0J1
serine protease high-temperature requirement A plays an indirect role in the maturation process of SpeB
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.88
-
benzyloxycarbonyl-Glu-Phe
-
-
0.22
-
benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
pH 4.27
0.262
-
benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
pH 6.35
0.494
-
benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
pH 4.49
2.28
-
benzyloxycarbonyl-Lys-Phe
-
-
0.193
-
benzyloxycarbonyl-Val-Arg-4-methylcoumarinyl-7-amide hydrochloride
-
-
-
0.422
-
N-benzoyl-Gly-p-nitrophenyl ester
-
-
0.132
-
N-benzyloxycarbonyl-Ala-p-nitrophenyl ester
-
-
0.0236
-
N-benzyloxycarbonyl-Gly-p-nitrophenyl ester
-
-
0.588
-
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
at pH 7.25
-
0.605
-
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
at pH 6.73
-
0.637
-
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
at pH 6.99
-
0.664
-
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
at pH 6.21
-
0.667
-
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
at pH 5.53
-
5.05
-
Nalpha-benzyloxycarbonyl-Lys-Phe
-
-
-
2.64
-
Nalpha-benzyloxycarbonyl-Nepsilon-t-butyloxycarbonyl-Lys-Phe
-
-
0.063
-
p-nitrobenzyloxycarbonyl-Gly-p-nitrophenyl ester
-
-
0.438
-
t-butyloxycarbonyl-Gly-p-nitrophenyl ester
-
-
-
0.61
-
tert-butyloxycarbonyl-Ala-p-nitrophenyl ester
-
-
0.334
-
cinnamoyl-Gly-p-nitrophenyl ester
-
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
effect of pH-value on the Km-value for benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
additional information
-
additional information
-
effect of methanol of Km-value for N-benzyloxycarbonyl-L-Ala, p-nitrophenyl alpha-N-benzyloxycarbonyl-L-Lys and N-benzyloxycarbonyl-Gly
-
additional information
-
additional information
-
effect of pH-value on the Km-value for phenyl alpha-N-benzyloxycarbonyl-L-lysinate
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.3
-
benzyloxycarbonyl-Glu-Phe
-
-
29.7
-
benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
pH 4.27
89.8
-
benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
pH 4.49
142
-
benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
pH 6.35
1.09
-
benzyloxycarbonyl-Lys-Phe
-
-
0.042
-
benzyloxycarbonyl-Val-Arg-4-methylcoumarinyl-7-amide hydrochloride
-
-
-
0.21
-
N-benzoyl-Gly-p-nitrophenyl ester
-
-
118
-
N-benzyloxycarbonyl-Ala-p-nitrophenyl ester
-
-
9.4
-
N-benzyloxycarbonyl-Gly-p-nitrophenyl ester
-
-
176
-
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
at pH 5.53
-
178
-
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
at pH 6.73
-
182
-
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
at pH 6.21
-
190
-
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
at pH 6.99
-
5.05
-
Nalpha-benzyloxycarbonyl-Lys-Phe
-
-
-
174
-
Nalpha-benzyloxycarbonyl-Lys-phenyl ester
-
at pH 7.25
8.6
-
Nalpha-benzyloxycarbonyl-Nepsilon-t-butyloxycarbonyl-Lys-Phe
-
-
1.15
-
p-nitrobenzyloxycarbonyl-Gly-p-nitrophenyl ester
-
-
0.147
-
t-butyloxycarbonyl-Gly-p-nitrophenyl ester
-
-
-
4.31
-
tert-butyloxycarbonyl-Ala-p-nitrophenyl ester
-
-
1.52
-
cinnamoyl-Gly-p-nitrophenyl ester
-
-
additional information
-
additional information
-
effect of pH-value on the turnover numer for benzyloxycarbonyl-Lys-p-nitrophenyl ester
-
additional information
-
additional information
-
effect of pH-value on the turnover number for phenyl alpha-N-benzyloxycarbonyl-L-lysinate
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
inhibition kinetics with Spi and Spe B pro-peptide
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
341
-
-
protease activity substrate azocasein
378
-
-
protease activity substrate proSPE B C47S mutant
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
12000
-
-
pro-sequence, gel filtration
28000
-
-
mature enzyme, gel filtration
28000
-
-
active enzyme, SDS-PAGE
28000
-
-
active mature enzyme, SDS-PAGE
28000
-
-
mature enzyme, SDS-PAGE
28000
-
-
mature enzyme or C192S mutant enzyme, SDS-PAGE
28000
-
P0C0J1
mature SpeB, SDS-PAGE
28000
-
-
SDS-PAGE, mature form
32000
-
-
high-speed equilibrium ultracentrifugation
32000
-
-
ultracentrifugation
33590
-
-
determination of amino acid composition
35000
-
-
SDS-PAGE
40000
-
-
inactive pro-enzyme, SDS-PAGE
40000
-
P0C0J1
precursor proSpeB, SDS-PAGE
40000
-
-
SDS-PAGE, zymogen
160000
-
-
gel filtration
additional information
-
-
primary structure
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 28000, mature enzyme, SDS-PAGE
?
-
x * 40000, immature zymogen, x * 28000, mature processed enzyme
?
-
x * 42000, immature zymogen, x * 28000, mature processed enzyme
?
-
x * 28000, mature enzyme; x * 40000, proenzyme, estimated from amino acid sequence
?
-
x * 28000, active enzyme, SDS-PAGE
?
Streptococcus pyogenes A-20
-
x * 42000, immature zymogen, x * 28000, mature processed enzyme
-
?
Streptococcus sp. MGAS315, Streptococcus sp. RGAS053
-
x * 28000, active enzyme, SDS-PAGE
-
additional information
-
the recombinant 12 kDa pro-sequence domain of the enzyme directs the folding of the mature enzyme, interaction overview
additional information
-
primary, and tertiary structure
additional information
-
secondary structure comparison of Spe B pro-peptide and Spi, overview
additional information
Streptococcus pyogenes B220
-
secondary structure comparison of Spe B pro-peptide and Spi, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
SpeB is secreted as a 40000 Da proenzyme that is converted into a mature 28000 Da active proteinase by autocatalytic cleavage
proteolytic modification
-
the enzyme performs autolytic processing to the 28 kDa mature protein, the 12 kDa pro-sequence domain, residues 28-145, directs the folding of the mature enzyme, overview
proteolytic modification
-
the enzyme performs autolytic processing to the mature 28 kDa protein by removal of an about 117 amino-acid peptide from the N-terminus
proteolytic modification
-
SPE B produced from group A Streptococcus (GAS) is released extracellularly to culture medium as a zymogen (proSPE B) with a molecular mass of 40 kDa. The conversion of proSPE B to the 28 kDa active mature SPE B (mSPE B) is achieved by autoproteolysis and exogenous proteases
side-chain modification
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autocatalytic maturation of the zymogen proceeds through the sequential appearance of at least six intermediates, resulting from cleavage after Lys26, Asn41, Lys101, Ala112 and Lys118
side-chain modification
-
complete removal of the 118 amino acids from the SCP zymogen results in formation of SCP
side-chain modification
-
autocatalytic processing of the 40000 Da zymogen to the 28000 Da mature form
side-chain modification
-
-
proteolytic modification
Streptococcus pyogenes A-20
-
the enzyme performs autolytic processing to the mature 28 kDa protein by removal of an about 117 amino-acid peptide from the N-terminus
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side-chain modification
Streptococcus pyogenes B220
-
autocatalytic maturation of the zymogen proceeds through the sequential appearance of at least six intermediates, resulting from cleavage after Lys26, Asn41, Lys101, Ala112 and Lys118
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side-chain modification
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
analysis of a crystal structure model of the zymogen
-
hanging drop vapour diffusion method, the crystal structure of the C47S mutant zymogen 40000 Da form expressed in Escherichia coli and its SeMet-substituted form, at 1.6 A resolution, reveals that the protein is a distant homologue of the papain superfamily
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purified recombinant mutant C47S, X-ray diffraction crystal structure determination and analysis at 1.6 A resolution
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pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
9.5
-
unstable below pH 4.5 and above pH 9.5
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
0.1 N HCl, 2 h, denaturation of the zymogen
60
-
-
irreversible inactivation
100
-
-
10 min, inactivation
100
-
-
pH 6.7, 10 min, denaturation of the zymogen
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0.1 N HCl or 0.01 N NaOH, room temperature, 2 h, denaturation
-
0.1 N HCl, 2 h, denaturation of the zymogen
-
0.5% SDS, denaturation
-
8 M urea plus reducing agent, 20% of proteolytic activity is provided
-
EDTA, 0.001 M, stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for at least 2 years
-
stored under nitrogen, 0.01 mM EDTA, 3-5% loss of activity per week
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
HiTrap SP column chromatography, and G75 Sephadex gel filtration
-
native mature Spe B by ammonium sulfate fractionation, dialysis, and ion exchange chromatography, recombinant His-tagged Spe B propeptide and SpeB mutant C47S from Escherichia coli
-
Ni2+-chelating column chromatography
-
recombinant His-tagged wild-type and mutant C192S enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the wild-type enzyme autoprocesses during purification to the mature 28 kDa protein
-
recombinant pro-sequence domain and refolded mature enzyme from Escherichia coli by affinity chromatography
-
recombinant wild-type and inactive mutant enzyme from Escherichia coli by affinity chromatography
-
the proteins are purified by Ni2+-chelating chromatography with a gradient of 20-200 mM imidazole. The proteins are concentrated by ultrafiltration using a 10 kDa cutoff membrane and then exchanged with phosphate-buffered saline
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
C192S mutant expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3)pLyS cells
-
expression in Escherichia coli, the zymogen proSCP is secreted to the Escherichia coli periplasm followed by subsequent cleavage of the signal peptide
-
expression of 12 kDa pro-sequence domain of the enzyme in Escherichia coli, expression of mature enzyme in Escherichia coli in inclusion bodies
-
expression of His-tagged wild-type and mutant C192S enzymes in Escherichia coli strain BL21(DE3)
-
expression of mutant C47S
-
expression of wild-type and inactive mutant enzyme in Escherichia coli strain BL21(DE3) and in A-549 cells
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gene speB, native expression pattern, expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha
-
genes speB and spi, nucleotide and amino acid sequence determination, analysis and comparison, co-expression of immature Spe B and Spi in Streptococcus pyogenes, Spi is similar to the pro-peptide of Spe B, overview, overexpression of His-tagged Spe B propeptide and SpeB mutant C47S in Escherichia coli
-
IdeS GST-fusion protein is expressed in Escherichia coli BL21
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C192S
-
lacks protease activity
C192S
-
no autocatalytic processing of the 40000 Da zymogen to the 28000 Da mature form, no proteolytic activity
C47S
-
crystal structure analysis
C47S
-
site-directed mutagenesis, inactive mutant
C47S
-
inactive mutant
D9N
-
protease activity (microgram/min/mg) substrate azocasein: 256, substrate proSPE B C47S mutant: 250, compared to wild-type 341 and 378, respectively
G136A
-
protease activity (microgram/min/mg) substrate azocasein: 22.3, substrate proSPE B C47S mutant: 8.1, compared to wild-type 341 and 378, respectively
G163S
-
protease activity (microgram/min/mg) substrate azocasein: 348, substrate proSPE B C47S mutant: 385, compared to wild-type 341 and 378, respectively
G163S/A172S
-
protease activity (microgram/min/mg) substrate azocasein: 286, substrate proSPE B C47S mutant: 236, compared to wild-type 341 and 378, respectively
G239D
-
protease activity (microgram/min/mg) substrate azocasein: 35.3, substrate proSPE B C47S mutant: 20, compared to wild-type 341 and 378, respectively
V189A
-
protease activity (microgram/min/mg) substrate azocasein: 2.6, substrate proSPE B C47S mutant: 0.9, compared to wild-type 341 and 378, respectively
W212A
-
protease activity (microgram/min/mg) substrate azocasein: 1.2, substrate proSPE B C47S mutant: 0.9, compared to wild-type 341 and 378, respectively
W214A
-
protease activity (microgram/min/mg) substrate azocasein: 0.8, substrate proSPE B C47S mutant: 0.8, compared to wild-type 341 and 378, respectively
C192S
Streptococcus pyogenes A-20
-
inactive mutant
-
C47S
Streptococcus pyogenes B220
-
site-directed mutagenesis, inactive mutant
-
G308S
-
behaviour is similar to the wild type enzyme
additional information
-
construction of an isogenic inactive mutant strain M6
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
refolding of denatured recombinant mature wild-type enzyme from inclusion bodies in 100 mM Na-acetate, pH 4.5, 8 M urea, 10 mM DTT, and 280 mM NaCl, by rapid dilution 1:20 into phosphate buffered saline, pH 7.4, with 10 mM DTT
-
90% renaturation provided the denatured zymogen is solubilized with urea or guanidinium chloride and given time to refold
-