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Bioactive Peptides and Enzymes : Their Stability, Assembly and Function

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Title Bioactive Peptides and Enzymes : Their Stability, Assembly and Function
 
Creator Sharma, Kanika
 
Subject Structural Biology & Bioinformatics
 
Description Proteases probably arose at the earliest stages of protein evolution as simple destructive enzymes which were necessary for protein catabolism and generation of amino acids in primitive organisms. Proteolysis of peptide bonds is one of the most important enzymatic modification of proteins. In the earlier days, proteolysis was always associated with protein digestion involving digestive proteases of pancreatic and gastric origin but the interest in study of proteases was stimulated by the recognition that they are involved in the regulation of a number of physiological processes. One of these functions involves zymogen activation by‘limited proteolysis’. Certain proteins are synthesized as inactive precursors or zymogens and selective enzymatic cleavage of peptide bonds converts them into the physiologically active form (Figure 2). This is involved in various biological processes like blood coagulation, fibrinolysis, complement reaction, hormone production, development, differentiation, supramolecular assembly etc. All of these involve zymogen activation in one or more steps (Neurath 1976; Dawie and Fujikawa, 1975; Cabib and Farkas, 1971). The specificity of limited
proteolysis is best understood in terms of the three-dimensional structure of a protein substrate and of the attacking protease because the region of the protein substrate containing the susceptible peptide bond must fit the active site of the attacking protease in order for amino
acid residues of the substrate to interact with primary as well as secondary binding sites of the enzyme
 
Date 2015
 
Type Thesis
NonPeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/2511/1/Kanika_Sharma_thesis.pdf
Sharma, Kanika (2015) Bioactive Peptides and Enzymes : Their Stability, Assembly and Function. PhD thesis, JU.
 
Relation http://www.eprints.iicb.res.in/2511/