An active alpha'2beta2 derivative of tryptophean synthase formed by limited proteolysis.
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چکیده
منابع مشابه
Probing Conformational Feature of a Recombinant Pyruvate Kinase by Limited Proteolysis
Pyruvate kinase is a key enzyme in glycolytic pathway that catalyzes the transphosphorylation between phosphoenolpyruvate and ADP to yield ATP and Pyruvate. Geobacillus stearothermophillus has a stable pyruvate kinase with determined crystal structure that composed of four separate domains. Given that limited proteolysis experiments can be successfully used to probe conformational features of p...
متن کاملProbing protein structure by limited proteolysis.
Limited proteolysis experiments can be successfully used to probe conformational features of proteins. In a number of studies it has been demonstrated that the sites of limited proteolysis along the polypeptide chain of a protein are characterized by enhanced backbone flexibility, implying that proteolytic probes can pinpoint the sites of local unfolding in a protein chain. Limited proteolysis ...
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Bovine pancreatic deoxyribonuclease A was selectively cleaved by digestion with a-chymotrypsin under carefully controlled conditions. The peptide bond in DNase A between tryptophan residue 178 and serine 179 was quantitatively hydrolyzed in less than 15 min by 0.5 % ac-chymotrypsin at pH 8.5 and 4” when divalent metal ions were absent. The modified DNase A (DNase A (l-178,179-257)) was composed...
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Limited or regulatory proteolysis plays a critical role in many important biological pathways like blood coagulation, cell proliferation, and apoptosis. A better understanding of mechanisms that control this process is required for discovering new proteolytic events and for developing inhibitors with potential therapeutic value. Two features that determine the susceptibility of peptide bonds to...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34609-4