3.4.21.B1: hyaluronan-binding serine protease
This is an abbreviated version!
For detailed information about hyaluronan-binding serine protease, go to the full flat file.
Word Map on EC 3.4.21.B1
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3.4.21.B1
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marburg
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fibrinolysis
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haemostasis
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nonmedullary
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autoactivation
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pro-urokinase
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fnmtc
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medicine
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srgap1
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analysis
- 3.4.21.B1
-
marburg
-
fibrinolysis
-
haemostasis
-
nonmedullary
-
autoactivation
- pro-urokinase
-
fnmtc
- medicine
-
srgap1
- analysis
Reaction
endopeptidase activity. Cleaves C-terminal site of Lys and Arg =
Synonyms
factor seven activating protease, factor VII activating protease, factor VII-activating protease, FASP, FSAP, gelatinolytic serine proteinase, HABP, HABP2, hyaluronan binding protein 2, hyaluronan-binding protease, hyaluronic acid-binding protease, PHBP, PHBSP, plasma hyaluronan-binding protein, S01.033
ECTree
3.4.21.B1 hyaluronan-binding serine proteaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.4.21.B1 - hyaluronan-binding serine protease
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
C1 esterase inhibitor
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inhibits autoactivation at physiological concentrations
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inhibitor C1
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C1 inhibitor of the serpin family, forms a complex with the enzyme, 50% inhibition at 0.001 mg/ml
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PPACK
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potent serine protease inhibitor, inhibits autoactivation at physiological concentrations
alpha2-antiplasmin
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potently inhibits amidolytic activity of FSAP, but no complex formation can be observed
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Aprotinin
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potent serine protease inhibitor, inhibits autoactivation at physiological concentrations
C1 inhibitor
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potently inhibits amidolytic activity of FSAP, but no complex formation can be observed
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KPI domain of amyloid-beta precursor protein
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complete inhibition at 0.012 mg/ml
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KPI domain of amyloid-beta precursor protein
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complete inhibition at 0.012 mg/ml
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KPI domain of amyloid-beta precursor protein
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complete inhibition at 0.012 mg/ml
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KPI domain of amyloid-beta precursor protein
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complete inhibition at 0.012 mg/ml
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plasminogen activator inhibitor-1
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potently inhibits amidolytic activity of FSAP, FSAP-plasminogen activator inhibitor-1 complex formation. Residue Arg346 is a critical recognition element on plasminogen activator inhibitor-1 for interaction with FSAP. RNA, but not DNA, fragments (more than 400 nucleotides in length) dramatically enhance reactivity of plasminogen activator inhibitor-1 with FSAP. Reactivity can be also enhanced by vitronectin. Also antagonizes FSAP-driven inhibition of vascular smooth muscle cell proliferation
Protease nexin-1
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inhibits FSAP enzymatic activity, which leads to the loss of the inhibitory effect of FSAP on platelet-derived growth factor-BB-mediated DNA synthesis and mitogen-activated protein kinase phosphorylation in vascular smooth-muscle cells. The FSAP-protease nexin-1 complex binds to the low-density lipoprotein receptor-related protein and is subsequently internalized. This binding is inhibited by receptor associated protein as well as heparin. The FSAP-inhibitor complexes are internalized via low-density lipoprotein receptor-related protein without influencing the platelet-derived growth factor-BB signal transduction pathway
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additional information
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alpha1-proteinase inhibitor and antithrombin III have no effect, no complex formation is observed
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additional information
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complex formation of FSAP with inhibitors results in rapid internalization of the complexes by low-density lipoprotein receptor-related protein via receptor-mediated endocytosis
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