Term
Specific Acid-Base Catalysis |
|
Definition
Involves the constituents of water donation of a proton by the hydronium ion [H3O+], or the acceptance of a proton by the hydroxyl ion [OH-]. |
|
|
Term
General Acid-Base Catalysis |
|
Definition
If the donor molecule is a weak acid or the abstracting molecule a weak base (like a reactive amino acid side chain). |
|
|
Term
|
Definition
When some of the energy of binding substrate within the active site is used to generate a conformational change in the shape of the active site. -In such a mechanism the conformational change distorts the substrate into a more reactive
shape resembling the transition state. |
|
|
Term
|
Definition
Results when a covalent enzyme-substrate intermediate is formed during the course of the reaction.
-Catalysis results if this covalent intermediate is more reactive toward the final acceptor molecule than was the original substrate. -serine proteases cleave peptide bonds using this mechanism, distinct from carboxypeptidases. |
|
|
Term
|
Definition
[Products]/[Reactants]=[E][S]/[ES]=k-1/k1 |
|
|
Term
|
Definition
=(k-1+k2)/k1
-[S] which gives 1/2(Vmax) -when k-1>>k2 then Km~KD -a measure of the affinity of the enzyme for the substrate, the lower the Km the higher the affinity |
|
|
Term
|
Definition
I binds only to E, not ES -I increases the apparent Km for S -as [S] becomes large, I becomes less effective as an inhibitor -Vmax is unaffected by the inhibitor |
|
|
Term
Noncompetetive inhibitors |
|
Definition
I binds to E & to ES
-apparent Km may be unchanged (common), or increased or decreased -Vmax is decreased -I interferes with conformational change, but has no effect on S binding. |
|
|
Term
|
Definition
I binds to ES -apparent Km is decreased -Vmax is decreased -k2 is lowered -the substrate binds the enzyme more readily but the catalytic site is not available to react with it. |
|
|
Term
Michaelis-Menton Equation |
|
Definition
vo=Vmax[S]/Km+[S] Vmax is proportional to k2 & [Et] |
|
|
Term
|
Definition
Rate constant is determined by the free energy of activation, catalysts can reduce that |
|
|
Term
|
Definition
A protease. -carbonyl polarization & oxyanion stabilization is accomplished by coordination of the oxygen to an active site Zn2+. -an active site glutamate acts as the nucleophile |
|
|
Term
|
Definition
1. Initial rate assumption: [S]=the amount of S added -there is no P & therefore no reverse reaction 2. Steady state assumption: The concentration of [ES] is nearly constant during most of the time P is being formed. |
|
|