462a_prac_prob_7_2013_key

You do michaelis menten kinetics and find that km for

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Unformatted text preview: determine the amino-acid sequence of clypsin A. It is found to be homologous to trypsin and chymotrypsin. From sequence alignments, you can identify the key specificity pocket residues as Thr 189-Ala 216-Val 226. You later discover that the monkey has an isozyme of this serine protease, clypsin B, in which residue 189 is Ser instead of Thr. You do Michaelis-Menten kinetics and find that KM for clypsin B with FAVE is 2 times higher than KM for clypsin A with FAVE, while KM for clypsin B with FALE is 2 times lower than KM for clypsin A with FALE. Propose an explanation for these findings. The Thr to Ser replacement probably increases the size...
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