BSCI-2520 Lecture Notes - Lecture 14: Histidine, Oxyanion, Lysozyme

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Allostery and enzymes: can change one dimer of multimeric enzyme to convert from t to r state and affect the active site of the enzyme in both dimers (3 and 4 changes to structure) Inhibitors stabilize the t state and activators stabilize the r state. 2- group on ser14) and b (does not) A is more active than b and cleaves off glucoses, arg moves out of the active site. Has two domains and the parts of the active site are from different domains. Triad: asp102, his57, ser195; residue sits in the pocket: trypsin: lys, arg, elastase: ala, gly, val, serines use 1 alcohol group, threonines use 2 alcohols, aspartates use pair of asp, Glutamic acid uses glu and gln, thiol uses cys. His57 acts as an acid and donates a proton reaction part of reaction to the n, breaks peptide bond, then base. Asp102 stabilizes the active site by making reaction.

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