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Information on EC 3.4.24.29 - aureolysin
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3.4.24.29 aureolysinSpecify your search results
Word Map
- 3.4.24.29
- c3b
- plasminogen
-
thrombolytic
- plasmin
-
hemolytic
- clot
- fibrin
-
fibrinolytic
- streptokinase
-
staphylococcal
- properdin
-
complement-mediated
- fibrinogen
-
nephritic
-
decay-accelerating
- glomerulonephritis
-
fibrin-specific
-
cell-bound
-
c3nefs
-
fluid-phase
-
membranoproliferative
- cobra
-
mbl-associated
- masp-2
-
2-antiplasmin
- glomerulopathy
-
kringle
-
mannan-binding
-
plasminogen-activating
- alpha2-antiplasmin
-
reocclusion
- ficolins
- glu-plasminogen
- reteplase
-
amidolytic
- coagulase
-
opsonin
-
leukocidin
- hemoglobinuria
-
profibrinolytic
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residue. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus
Synonyms
c3 convertase, staphylokinase, aureolysin, aurwm, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aur
aurWM
C3 convertase
EC 3.4.24.4
-
-
formerly
-
EC 3.4.99.22
-
-
formerly
-
Proteinase, Staphylococcus aureus neutral
-
-
-
-
Staphylococcus aureus neutral protease
-
-
-
-
Staphylococcus aureus neutral proteinase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residue. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
39335-13-2
-
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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
alpha2-macroglobulin + H2O
?
-
processing of the inhibitor, the initial N-terminal hydrolysis of alpha2-macroglobulin by aureolysin does not affect the serpin inhibitory activity, cleavage within its exposed reactive loop is associated with a decreased inhibitory activity, down to 23% of the control inhibitor
-
-
?
Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
-
-
?
GWTLNSAGYLLGPHAIDNHRSFHDKYGLA-NH2 + H2O
Gly-Trp-Thr + Leu-Asn-Ser + Ala-Gly + Tyr + Leu + LGPHAIDNHRS + FHDKYG + Leu-Ala-NH2
-
i.e. galanin
-
-
?
Nalpha-furylacryloyl-Gly-Leu-NH2
?
-
Nalpha-furylacryloyl-Gly-Phe-NH2 is a better substrate than Fa-Gly-Leu-NH2
-
-
?
Nalpha-furylacryloyl-Gly-Phe-NH2
?
-
Nalpha-furylacryloyl-Gly-Phe-NH2 is a better substrate than Fa-Gly-Leu-NH2
-
-
?
plasminogen activator inhibitor-1 + H2O
?
-
processing of the inhibitor, the proteolytic degradation of PAI-1 by aureolysin is associated with a drastic decrease in its capacity to inhibit uPA, down to 7% of the inhibitory activity of the control PAI-1
-
-
?
pro-urokinase-type plasmin activator + H2O
2 chains of urokinase-type plasmin activator
-
human substrate, activation by cleavage into two enzyme chains, activity by wild-type strains 8325-4 and Newman, and clinical isolates, overview, no activity with N-terminal enzyme substrate mutants, overview
-
-
?
cathelicidin LL-37 + H2O
?
-
human antimicrobial peptide. Enzyme production by Staphylococcus aureus contributes to its resistance to the innate immune system of humans mediated by LL-37
-
-
?
cathelicidin LL-37 + H2O
?
-
human antimicrobial peptide, cleavage by enzyme at R19-I20, R23-I24, L31-V32
-
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b. In serum, the aureolysin-generated C3b is further degraded by host factors
both products are active
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b
both products are active
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b. In serum, the aureolysin-generated C3b is further degraded by host factors
both products are active
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b
both products are active
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity. It cleaves human galectin-3 (a beta-galactoside-binding lectin involved in immune regulation and antimicrobial defense) into mostly higher-molecular-mass fragments, suggesting that it primarily digested the more distant parts of the N-terminal collagen-like domain
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity. It cleaves human galectin-3 (a beta-galactoside-binding lectin involved in immune regulation and antimicrobial defense) into mostly higher-molecular-mass fragments, suggesting that it primarily digested the more distant parts of the N-terminal collagen-like domain
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin
-
hydrolysis of bonds in which the NH2-group of hydrophobic amino acids is involved, no hydrolysis of Phe24-Phe25
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin
-
cleaves at His5-Leu6, His10-Leu11, Ala14-Leu15, Tyr16-Leu17, Gly23-Phe24, Phe25-Tyr26
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin
-
hydrolysis of bonds in which the NH2-group of hydrophobic amino acids is involved, no hydrolysis of Phe24-Phe25
-
-
?
SspA zymogen + H2O
?
-
aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65, mechanism, overview
-
-
?
SspA zymogen + H2O
?
-
SspA is a serine protease secreted by Staphylococcus aureus as inactive zymogen, aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65
-
-
?
SspA zymogen + H2O
?
-
aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65, mechanism, overview
-
-
?
SspA zymogen + H2O
?
-
SspA is a serine protease secreted by Staphylococcus aureus as inactive zymogen, aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65
-
-
?
additional information
?
-
-
specificity for peptide bonds on the N-terminal side of large hydrophobic residues
-
-
?
additional information
?
-
-
protease II exhibits esterase activity, using N-benzoyl-L-Tyr ethyl ester as substrate, no activity of protease I
-
-
?
additional information
?
-
-
activates the precursor of another protease secreted by the same organism, staphylococcal protease
-
-
?
additional information
?
-
-
the aur null mutant strain causes the same immune reaction in mice as the wild-type strain, overview
-
-
?
additional information
?
-
-
aureolysin does not hydrolyze GKHKNKGKKNGKHNGWK and HKHGHGHGKHKNKGKKN
-
-
?
additional information
?
-
-
Aureolysin collaborates with host factors to inactivate C3b
-
-
?
additional information
?
-
-
pulmonary surfactant protein-A from human host lung is no substrate for aureolysin from Staphylococcus aureus, but for staphylopain A, EC 3.4.22.48
-
-
?
additional information
?
-
-
Aureolysin collaborates with host factors to inactivate C3b
-
-
?
additional information
?
-
-
protease II exhibits esterase activity, using N-benzoyl-L-Tyr ethyl ester as substrate, no activity of protease I
-
-
?
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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
cathelicidin LL-37 + H2O
?
-
human antimicrobial peptide. Enzyme production by Staphylococcus aureus contributes to its resistance to the innate immune system of humans mediated by LL-37
-
-
?
Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
-
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b. In serum, the aureolysin-generated C3b is further degraded by host factors
both products are active
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b. In serum, the aureolysin-generated C3b is further degraded by host factors
both products are active
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity. It cleaves human galectin-3 (a beta-galactoside-binding lectin involved in immune regulation and antimicrobial defense) into mostly higher-molecular-mass fragments, suggesting that it primarily digested the more distant parts of the N-terminal collagen-like domain
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity. It cleaves human galectin-3 (a beta-galactoside-binding lectin involved in immune regulation and antimicrobial defense) into mostly higher-molecular-mass fragments, suggesting that it primarily digested the more distant parts of the N-terminal collagen-like domain
-
-
?
SspA zymogen + H2O
?
-
aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65, mechanism, overview
-
-
?
SspA zymogen + H2O
?
-
aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65, mechanism, overview
-
-
?
additional information
?
-
-
activates the precursor of another protease secreted by the same organism, staphylococcal protease
-
-
?
additional information
?
-
-
the aur null mutant strain causes the same immune reaction in mice as the wild-type strain, overview
-
-
?
additional information
?
-
-
Aureolysin collaborates with host factors to inactivate C3b
-
-
?
additional information
?
-
-
Aureolysin collaborates with host factors to inactivate C3b
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Zn2+
additional information
Co2+
-
slight stimulation of protease I, protease II inactive in presence of
Co2+
-
reactivates 1,10-phenanthroline inactivated enzyme with 160% of the activity of the native enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha2-Macroglobulin
-
a regulatory serpin, the initial N-terminal hydrolysis of alpha2-macroglobulin by aureolysin does not affect the serpin inhibitory activity, cleavage within its exposed reactive loop is associated with a decreased inhibitory activity, down to 23% of the control inhibitor
-
Co2+
-
protease II inactive in presence of, protease I slightly stimulated
DFP
-
1.0 mM, 30 min, 20°C, activity of protease I is reduced by 10%, activity of protease II by 30%
NaCl
-
50% reduction of activity at 0.3 M for protease I and 0.5 M for protease II
plasminogen activator inhibitor-1
-
PAI-1, a regulatory serpin, interaction analysis with aureolysin, overview, the proteolytic degradation of PAI-1 by aureolysin is associated with a drastic decrease in its capacity to inhibit uPA, down to 7% of the inhibitory activity of the control PAI-1
additional information
-
protease I is not significantly affected by SH-reducing, SH-inactivating or metal-complexing agents
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Reducing agents
-
protease II active only in presence of reducing agents such as cysteine, 2-mercaptoethanol or sodium thioglycollate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
analysis of polymorphisms in vancomycin-resistant strains, VRS1, HIP11714, strain VRS2, HIP11983 and strain VRS3, HIP13170 reveals a high degree of gene polymorphism. The aur gene is subject to stronger purifying selection than the multilocus sequence typing genes MLST. Proper enzymatic activity and specificity of aureolysin is very important in the processing of other staphylococcal proteins
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the enzyme is expressed and secreted in the course of human and mouse infection, overview
brenda
additional information
-
the enzyme is expressed and secreted in the course of human and mouse infection, overview
brenda
additional information
-
the enzyme is expressed and secreted in the course of human and mouse infection, overview
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
the sigB mutant strain overexpresses the surface-anchored protein Bap, that is essential for biofilm formation in the model strain. Staphylococcus aureus completely inhibits the biofilm formation of the mutant strain via Aur and SspA, two proteases that are overexpressed in the sigB mutant strain and are capable of degrading Bap
metabolism
physiological function
metabolism
-
four major extracellular proteases of Staphylococcus aureus are potent complement inhibitors: cysteine proteases staphopain A and staphopain B, the serine protease V8, and the metalloproteinase aureolysin cause a drastic decrease in the haemolytic activity of serum, whereas two serine-protease like enzymes, SplD and SplE, have no effect. The four enzymes inhibit all pathways of complement due to the efficient degradation of several crucial components
metabolism
-
four major extracellular proteases of Staphylococcus aureus are potent complement inhibitors: cysteine proteases staphopain A and staphopain B, the serine protease V8, and the metalloproteinase aureolysin cause a drastic decrease in the haemolytic activity of serum, whereas two serine-protease like enzymes, SplD and SplE, have no effect. The four enzymes inhibit all pathways of complement due to the efficient degradation of several crucial components
-
physiological function
-
extracellular proteases Aur and SspA inhibit protein-dependent biofilm formation by Staphylococcus aureus, detailed overview
physiological function
-
Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to mediate immune evasion and is a potent complement inhibitor dependent on its proteolytic activity. Aureolysin effectively inhibits phagocytosis and killing of bacteria by neutrophils in the human host, e.g. in U937 cells, aureolysin inhibits C3b deposition and C5a generation, overview. Aureolysin is essential and sufficient for C3 cleavage by bacterial supernatant, but acts in synergy with host regulators to inactivate C3 thereby effectively dampening the host immune response. Aureolysin acts as a C3 convertase
physiological function
-
the enzyme interacts with the host tissue components in vitro to modulate host defense mechanisms and likely increase bacterial survival, but is not involved in the breakdown of first line of innate immune defense agent, pulmonary surfactant protein-A, of human host lung cells
physiological function
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
physiological function
the enzyme is probably associated with efficient processing of the PROM protease (homolog of V8/SspA serine protease). Additionally, AurWM appeares to affect biofilm formation in an uncertain suppressive way
physiological function
-
Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to mediate immune evasion and is a potent complement inhibitor dependent on its proteolytic activity. Aureolysin effectively inhibits phagocytosis and killing of bacteria by neutrophils in the human host, e.g. in U937 cells, aureolysin inhibits C3b deposition and C5a generation, overview. Aureolysin is essential and sufficient for C3 cleavage by bacterial supernatant, but acts in synergy with host regulators to inactivate C3 thereby effectively dampening the host immune response. Aureolysin acts as a C3 convertase
-
physiological function
-
the enzyme is probably associated with efficient processing of the PROM protease (homolog of V8/SspA serine protease). Additionally, AurWM appeares to affect biofilm formation in an uncertain suppressive way
-
physiological function
-
the enzyme acts as host complement inhibitor
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A084FWR0_PSEDA
392
0
43299
TrEMBL
other Location (Reliability: 2)
D5BMI6_PUNMI
Puniceispirillum marinum (strain IMCC1322)
415
0
44676
TrEMBL
-
A0A3B0VET1_9ZZZZ
516
0
55965
TrEMBL
other Location (Reliability: 2)
E9P6N2_STREQ
403
0
45940
TrEMBL
-
A0A3B0U998_9ZZZZ
738
0
80928
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3B0UZV4_9ZZZZ
579
1
64146
TrEMBL
Secretory Pathway (Reliability: 1)
E9P6N3_STREQ
403
0
45974
TrEMBL
-
A0A3B0VTS5_9ZZZZ
431
0
47390
TrEMBL
Mitochondrion (Reliability: 3)
A0A7S9SSY3_STREQ
393
0
44986
TrEMBL
-
Q2FUX4_STAA8
Staphylococcus aureus (strain NCTC 8325 / PS 47)
498
0
54986
TrEMBL
-
SSPA_STAA8
Staphylococcus aureus (strain NCTC 8325 / PS 47)
336
0
36326
Swiss-Prot
-
