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biochem test3 08 002 - 12 What is the Michaelis-Menton...

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Unformatted text preview: 12). What is the Michaelis-Menton expression under uncompetitive inhibition? _ KVmadSl 1: _ M+a'[S] ._ . .. V [S] _ max V0 — aKM +a[S] \ib" \iWW‘ [5'3 /V__V,..xts1 M ' ° aKM+181 . \me' [Q- mime] "KM+w1 V : V...,.181 ° KM+181 13). What is the ’Lineweaver-Burke expression under competitive inhibition? 1 _ ocKM 1 + 01' .Lii ' \hmeS3 V0 — Vmax [S] + Vmax ’ \IQ // 1 _(xKM 1 1 otKV‘HrCQ v—fvflw To i ‘J‘Wt‘CEQ = Vm[S] A» f oxkfsAc /’ \T‘M KM+181 \lo \hmfig so 14). What gets put into the oxyanion hole in the active site of serine proteases? \)0 a. A water molecule used in the nucleophilic attack on the peptide substrate b. The C=O group in the sidechain of an Asn residue in the substrate‘peptide c. The C=O group from the substrate peptide backbone yThe 0- generated during attack of the substrate peptide backbone C=O e. The OH group of the side chain of the active site Ser residue 15). The Michaelis constant, KM, is 7 a. The rate at which the Michaelis complex goes on to form product b The rate at which the Michaelis complex IS formed 91‘ he concentration at which the Va is half maximal d. The concentration at which the v0 is maximal e. The concentration at which the initial velocity, Va, is rate limiting 16). A measure of the cataiytic efficiency of an enzymatic reaction is fie" kca: 19- Vmax/[Eh :‘kf/Wt &L (09? i \{M . i.fi___] ...
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