By Borivoj Keil
Specificity of Proteolysis offers a survey and conclusions at the motion or proteinases - enzymes that are cleaving proteins or peptides. The specificity of proteinases that's decided because the series of amino acids on the cleavage website of a substrate, is a crucial standards to settle on an enzyme as software in protein study. each time one is seeking an enzyme to behave at an outlined website or to offer outlined cleavage items one will locate accomplished details during this paintings. entire information regarding greater than 280 endopeptidases that are in line with the database LYSIS together with a calculation software to figure out cleavage websites, is given within the book.
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Additional info for Specificity of Proteolysis
Example text
Poly-L-arginine is not cleaved (0811). In arginine-rich histone cleavages were observed ofless than 10% of arginyl bonds (1038) and no cleavage of Arg in PI 45 lysyl bonds. In contrast with this exists a solitary observation of cleavages of both arginyl and lysyl bonds in histone H2A (0133). No cleavage was observed of the sequences Lys-Arg-Ser and Lys-Arg-Gln (complement fragment B6) (0223); in the sequences Arg-Arg-Gly (elongation factor 1; 0190) and Arg-Arg-Ala (glucagon; 0811) the Arg-Arg bond remains resistant.
5 Influence of Subsites Some dipeptidic sequences occur twice in the three standard polypeptides. Thus CG, HL and LV are repeated twice in the B-chain of insulin; LY, VC and VE exist in both the insulin A- and B-chain and VE and FV in both the B-chain and glucagon. If the specificity of a given enzyme would depend only on subsites PI and PI', it should cleave in both sites or leave both of them intact. The survey in Tables 5-7 shows that for many endopeptidases this is not the case. In the following discussion we will take in account only clear-cut examples where a given dipeptide is cleaved (C/G) in one site and remains intact (C-G) in the other one.
These examples confirm the general rule of proteolytic cleavage: short-time digestion, low temperature and high substrate-enzyme ratio are to be preferred to obtain highly specific cleavages. 2 Available Data on Cleavages oflnsulin Chains and Glucagon In Tables 5-7 the results are summarized (still not exhaustively) of experimental studies to determine the specificity of 137 endopeptidases on A-, B-chains of insulin and glucagon. Oxidized B-chain is the most frequently used substrate (132 proteinases); only 10 proteinases were studied on all 3 substrates.