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.and probably the amino acid which attacks the carbonyl C in the substrate, forming the acyl-intermediate. llmodification of the enzyme with tos-L-Phe-chloromethyl ketone inactives the enzyme with a 1:1 stoichiometry which results in a modified Hisllcomparison of the primary sequence of many proteases show that three residues are invariant: Ser 195, His 57, Asp 102llsite-specific mutagenesis show that if Ser 195 is changed to Ala 195, the enzymatic activity is almost reduced to background.l
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