Sandbox Reserved 1091
From Proteopedia
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The '''domain structure of ASP''' consists of the propeptide, the catalytic subtilisin-like domain, and the P-domain. The ASP molecule have two mean regions: an N-terminal region extending from Gly-3 to Pro-431 and forming the <scene name='82/829344/The_subtilisin_domain/2'>subtilisin domain</scene>, and a C-terminal region extending from Leu-432 to His-595 and forming the <scene name='82/829344/The_p-domain/2'>P-domain</scene>. | The '''domain structure of ASP''' consists of the propeptide, the catalytic subtilisin-like domain, and the P-domain. The ASP molecule have two mean regions: an N-terminal region extending from Gly-3 to Pro-431 and forming the <scene name='82/829344/The_subtilisin_domain/2'>subtilisin domain</scene>, and a C-terminal region extending from Leu-432 to His-595 and forming the <scene name='82/829344/The_p-domain/2'>P-domain</scene>. | ||
- | Moreover, we can find three <scene name='82/829344/Calcium_binding_sites/2'>Ca2+ Binding Sites</scene> in the ASP Structure (Ca1, Ca2 and Ca3). <scene name='82/829344/Ca1_et_ca2/4'>Ca1 and Ca2</scene> are situated in the N-terminal domain, and <scene name='82/829344/Ca3/3'>Ca3</scene> is situated in the C-terminal domain. It were assigned to ASP based on electron density, counter charges, and coordination. But in contrary to | + | Moreover, we can find three <scene name='82/829344/Calcium_binding_sites/2'>Ca2+ Binding Sites</scene> in the ASP Structure (Ca1, Ca2 and Ca3). <scene name='82/829344/Ca1_et_ca2/4'>Ca1 and Ca2</scene> are situated in the N-terminal domain, and <scene name='82/829344/Ca3/3'>Ca3</scene> is situated in the C-terminal domain. It were assigned to ASP based on electron density, counter charges, and coordination. But in contrary to Kex2 ([[1r64]]), ASP contains no Ca2+ binding sites near its catalytic site. |
Those Ca2+ binding sites are important because ... | Those Ca2+ binding sites are important because ... | ||
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ASP has its highest activity at pH 7,5 and loses it after heating at 60° for 10 minutes. | ASP has its highest activity at pH 7,5 and loses it after heating at 60° for 10 minutes. | ||
- | Experiments have been done in order to establish the sensitivity of ASP to proteases. In has been found that the ASP protease activity was strongly attenuated by serine protease inhibitors ([http://en.m.wikipedia.org/wiki/Diisopropyl_fluorophosphate DFP], [http://fr.m.wikipedia.org/wiki/Fluorure_de_4-(2-aminoéthyl)benzènesulfonyle AEBSF]). Moreover, a soybean trypsin inhibitor was shown not to block the proteolytic action of ASP itself but could inhibit the [http://en.m.wikipedia.org/wiki/Vascular_permeability vascular permeability] enhancing activity that follows after injection of ASP into epithelial cells. <ref>Physicochemical and biological properties od an extracellular serine protease od Aeromonas sobria. Ritsuko Yokoyama, Yoshio Fujii et al., 2002 Japan.</ref> | + | Experiments have been done in order to establish the sensitivity of ASP to proteases. In has been found that the ASP protease activity was strongly attenuated by serine protease inhibitors ([http://en.m.wikipedia.org/wiki/Diisopropyl_fluorophosphate DFP], [http://fr.m.wikipedia.org/wiki/Fluorure_de_4-(2-aminoéthyl)benzènesulfonyle AEBSF]). Moreover, a soybean [http://en.wikipedia.org/wiki/Trypsin_inhibitor trypsin inhibitor] was shown not to block the proteolytic action of ASP itself but could inhibit the [http://en.m.wikipedia.org/wiki/Vascular_permeability vascular permeability] enhancing activity that follows after injection of ASP into epithelial cells. <ref>Physicochemical and biological properties od an extracellular serine protease od Aeromonas sobria. Ritsuko Yokoyama, Yoshio Fujii et al., 2002 Japan.</ref> |
This experimental finding suggests that epithelial trypsin-like proteases mediate the reaction causing enhanced vascular permeability. It is likely that ASP stimulates the secretion and maturation of epithelial trypsin proteases, thus enhancing vascular permeability. ASP could stimulate the [http://en/m.wikipedia.org/wiki/Bradykinin bradykinin]-releasing pathway, thus stimulating mast cells to release histamine and further enhance the vascular permeability. | This experimental finding suggests that epithelial trypsin-like proteases mediate the reaction causing enhanced vascular permeability. It is likely that ASP stimulates the secretion and maturation of epithelial trypsin proteases, thus enhancing vascular permeability. ASP could stimulate the [http://en/m.wikipedia.org/wiki/Bradykinin bradykinin]-releasing pathway, thus stimulating mast cells to release histamine and further enhance the vascular permeability. |
Revision as of 08:53, 16 January 2020
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The serine protease from Aeromonas sobria
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References
- ↑ Fuller RS, Brake A, Thorner J. Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease. Proc Natl Acad Sci U S A. 1989 Mar;86(5):1434-8. PMID:2646633
- ↑ Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Takahisa Imamura et al., 2017
- ↑ http://www.msdmanuals.com/professional/critical-care-medicine/sepsis-and-septic-shock/sepsis-and-septic-shock
- ↑ Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. Kobayashi H et al. Biol. Chem. 290(17):11130-43 (2015)
- ↑ Aeromonas sobria serine protease (ASP): a subtilisin family endopeptidase with multiple virulence activities. Imamura T, Murakami Y, Nitta H. Biol. Chem. 398 1055-1068 (2017)
- ↑ Physicochemical and biological properties od an extracellular serine protease od Aeromonas sobria. Ritsuko Yokoyama, Yoshio Fujii et al., 2002 Japan.