Substrate specificity of SpoIIGA, a signal-transducing aspartic protease in Bacilli
نویسندگان
چکیده
منابع مشابه
Determination of aspartic protease gene dosage in the Onchocerca volvulusgenome
Aspartic proteases are a relatively small group of enzymes which express in various nematodes including Onchocerca volvulus. An estimation of the gene copy number corresponding to the OV7A clone, which contains a cDNA insert encoding approximately two-thirds of the entire coding sequence of aspartic protease of O. volvulus, was made by slot blot analysis in a closely related species O. gibsonig...
متن کاملSubstrate specificity of Tulane virus protease.
Tulane virus (TV) is a cultivable calicivirus isolated from rhesus monkeys. In this study, we characterized the substrate specificity of TV protease in trans using recombinant proteases and TV polyprotein fragments containing the predicted proteolytic cleavage sites. Cleavage products have been obtained from 4 of the 5 fragments containing (573)Q-S(574) between the helicase and 3A-like protein,...
متن کاملIn vitro reconstitution and substrate specificity of a lantibiotic protease.
Lacticin 481 is a lanthionine-containing bacteriocin (lantibiotic) produced by Lactococcus lactis subsp. lactis. The final steps of lacticin 481 biosynthesis are proteolytic removal of an N-terminal leader sequence from the prepeptide LctA and export of the mature lantibiotic. Both proteolysis and secretion are performed by the dedicated ATP-binding cassette (ABC) transporter LctT. LctT belongs...
متن کاملMicrobial Aspartic protease inhibitors
Aspartic proteases are relatively a small group of proteolytic enzymes. Over the last decade, they have received tremendous research interest as potential targets for pharmaceutical intervention as many have been shown to play significant roles in physiological and pathological processes. Despite numerous efforts, however, the only inhibitors for aspartic proteases currently in the market are d...
متن کاملSite-2 protease substrate specificity and coupling in trans by a PDZ-substrate adapter protein.
Site-2 proteases (S2Ps) are intramembrane metalloproteases that cleave transmembrane substrates in all domains of life. Many S2Ps, including human S2P and Mycobacterium tuberculosis Rip1, have multiple substrates in vivo, which are often transcriptional regulators. However, S2Ps will also cleave transmembrane sequences of nonsubstrate proteins, suggesting additional specificity determinants. Ma...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The Journal of Biochemistry
سال: 2011
ISSN: 1756-2651,0021-924X
DOI: 10.1093/jb/mvr027