3.4.24.29: aureolysin
This is an abbreviated version!
For detailed information about aureolysin, go to the full flat file.
Word Map on EC 3.4.24.29
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3.4.24.29
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c3b
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plasminogen
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thrombolytic
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plasmin
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hemolytic
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clot
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fibrin
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fibrinolytic
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streptokinase
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staphylococcal
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properdin
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complement-mediated
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fibrinogen
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nephritic
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decay-accelerating
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glomerulonephritis
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fibrin-specific
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cell-bound
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c3nefs
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fluid-phase
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membranoproliferative
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cobra
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mbl-associated
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masp-2
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2-antiplasmin
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glomerulopathy
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kringle
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mannan-binding
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plasminogen-activating
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alpha2-antiplasmin
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reocclusion
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ficolins
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glu-plasminogen
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reteplase
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amidolytic
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coagulase
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opsonin
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leukocidin
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hemoglobinuria
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profibrinolytic
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medicine
- 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
Reaction
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
Aur, aurWM, C3 convertase, EC 3.4.24.4, EC 3.4.99.22, Proteinase, Staphylococcus aureus neutral, Staphylococcus aureus neutral protease, Staphylococcus aureus neutral proteinase
ECTree
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Inhibitors
Inhibitors on EC 3.4.24.29 - aureolysin
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alpha2-Macroglobulin
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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
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Co2+
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protease II inactive in presence of, protease I slightly stimulated
DFP
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1.0 mM, 30 min, 20°C, activity of protease I is reduced by 10%, activity of protease II by 30%
NaCl
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50% reduction of activity at 0.3 M for protease I and 0.5 M for protease II
plasminogen activator inhibitor-1
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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
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protease I is not significantly affected by SH-reducing, SH-inactivating or metal-complexing agents
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