English Journal
- [New antivirals against hepatitis C virus].
- Kato N1, Muroyama R, Goto K.
- Nihon rinsho. Japanese journal of clinical medicine.Nihon Rinsho.2012 Apr;70(4):664-70.
- Recently, first direct acting antiviral (DAA) against hepatitis C virus (HCV) has just approved in Japan. It is a first generation protease inhibitor, telaprevir. Telaprevir inhibits HCV NS3 & 4A serine protease, and combination with pegylated-interferon and ribavirin has now become a standard o
- PMID 22568151
- Enteropeptidase, a type II transmembrane serine protease.
- Zheng XL1, Kitamoto Y, Sadler JE.
- Frontiers in bioscience (Elite edition).Front Biosci (Elite Ed).2009 Jun 1;1:242-9.
- Enteropeptidase, a type II transmembrane serine protease, is localized to the brush border of the duodenal and jejunal mucosa. It is synthesized as a zymogen (proenteropeptidase) that requires activation by another protease, either trypsin or possibly duodenase. Active enteropeptidase then converts
- PMID 19482641
- Rapid autocatalytic activation of the M4 metalloprotease aureolysin is controlled by a conserved N-terminal fungalysin-thermolysin-propeptide domain.
- Nickerson NN1, Joag V, McGavin MJ.
- Molecular microbiology.Mol Microbiol.2008 Sep;69(6):1530-43. doi: 10.1111/j.1365-2958.2008.06384.x. Epub 2008 Jul 30.
- SUMMARY: The Staphylococcus aureus proteolytic cascade consists of a metalloprotease aureolysin (Aur), which activates a serine protease zymogen proSspA, which in turn activates the SspB cysteine protease. As with other M4 metalloproteases, including elastase of Pseudomonas aeruginosa, the propeptid
- PMID 18673454
Japanese Journal
- Signal Peptidase Cleavage Site in the Processing of Pseudomonas aeruhginosa Preproelastase
- SHIBANO YUJI,INAGAKI KENJI,FUKUSHIMA JUN,KAWAMOTO SUSUMU,OKUDA KENJI,MORIHARA KAZUYUKI
- Journal of fermentation and bioengineering 78(4), 331-332, 1994-10-25
- … The extracellular elastase (33 kDa) of Pseudomonas aeruginosa is synthesized as a 53.6-kDa preproenzyme containing a long N-terminal propeptide, which is processed to the mature form via a 51-kDa proelastase. … No autoproteolytic processing of proelastase was expected to occur in these cells. … This confirms that the 51-kDa protein is proelastase and that the signal peptidase cleaves between Ala^<-175> …
- NAID 110002681937
- Binding Specificity of Anti-Human Pancreatic Elastase 1 Autoantibodies and Conjugation Forms of Elastase 1 in Serum.
- ASADA Hidehisa,KONO Masao,UCHIDA Kiyohisa,FUNAKOSHI Akihiro
- Journal of Clinical Biochemistry and Nutrition 16(1), 67-75, 1994
- … Anti-human pancreatic elastase 1 autoantibodies occurring in sera of patients with pancreatic diseases specifically bound elastase 1 but showed little binding with proelastase 1. … Binding of proelastase 1 to the autoantibodies was effectively elevated by tryptic digestion of the proelastase 1 for activation, suggesting that the autoantibodies recognized some conformational change from proelastase 1 to elastase 1. …
- NAID 130003670290
- Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and expression of the mutated lasB alleles in Escherichia coli show evidence for autoproteolytic processing of proelastase.
- MCIVER K. S.
- J.Bacteriol. 173, 7781-7789, 1991
- NAID 80006329915
Related Links
- ... chymotrypsinogen zymogen is cleaved by trypsin, the newly generated structure called a pi-chymotrypsin undergoes autolysis (self digestion), yielding active chymotrypsin. Proelastase, elastase, It is activated by cleavage through trypsin.
- the inert precursor of elastase, found in the pancreas. Want to thank TFD for its existence? Tell a friend about us, add a link to this page, add the site to iGoogle, or visit the webmaster's page for free fun content.
Related Pictures
