BCHE 395-11 2013 Enzymes Intro

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Unformatted text preview: te” •  TransiKon state intermediate is energe8cally unstable with respect to BOTH reactants (substrate) and product •  Can slide forward or back with equal chance when on “top” of the hill 25 E + S ⇌ [ES ⇌ ES⧧ ⇌ EP] ⇌ E + P Tends to be fast Generally the Rate limiKng step 26 Catalyst’s Role •  (1) Catalysts enhance reac8on rates by lowering ac8va8on energies •  (2) Catalysts permit the formaKon of transiKon state intermediates of lower energy (higher stability) than that for the uncatalyzed reacKon –  So, stabilizaKon of transiKon state of a reacKon by an enzyme suggests the enzymes has a higher binding affinity for the transi8on state intermediates than it does for the substrate OR product 27 Catalyst’s Role •  (3) Ac8ve site of enzymes are complementary in structure to the ac8vated complexes of the transi8on state intermediates •  But remember, non- covalent forces defining substrate- enzyme interacKons are similar in character to forces dictaKng protein conformaKon 28 Catalyst’s Role •  (4) Enzyme – substrate interacKons are not limited to acKve sites •  (5) Much of the catalyKc power of enzymes is ulKmately derived from...
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