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LIFE 210 (38)

Enzymes, the active site, mechanics of catalysis, apoptosis

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Colorado State University
Life Science
LIFE 210
Paul Laybourn

2 September History and Overview Research on how sugar is digested and fermented 1850’s – Pasteur, a “vitalist”, believed needed live cells 1897 – Buchner, a “mechanist” – cell free extracts work - Kühne, “enzyme” Greek for “in yeast” 1926 – Sumner, 1 to purify an enzyme, was a protein Enzymes Proteins Catalytic – unchanged Named generally by ending in “-ase” Why special (different from other catalysts) Very specific for substrates and chemical pathway Can be regulated Can “couple” reactions Business end – the “Active Site” Cleft or crevice Substrate fits into active site cleft R groups provide interactions, chemistry Multiple non covalent interactions Four main types of catalysis Acid-base Covalent intermediate Reaction intermediate stabilization Orientation/proximity Mechanisms of Catalysis – kinetics vs. thermodynamics Enzymes affect pathway and kinetics (rate) not thermodynamics Pathway independent Determines direction Enzymes can affect rate 10 – to – 10 – fold (usually around 10 – to - 10 – fold) S‡ is transition state ΔG‡ is activation energy ΔΔG‡ is how much the enzyme changes the necessary activation energy
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