CAS BI 108 Chapter Notes - Chapter 8.4: Covalent Bond, Enzyme, Reaction Rate
11 Mar 2014
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Document Summary
Enzymes can orient substrates: need to proper orientation to interact. Enzymes can induce strain in the substrate: stretching the bonds between monomers, to make bonds unstable and more reactive to the substrate. Enzymes can temporarily add chemical groups to substrates: side chains can make substrates more chemically reactive. Acid-base catalysis: acidic or basic side chains of amino acids in active site transfer h+ to or from the substrate to destabilize covalent bond. Covalent catalysis: functional group forms a temporary covalent bond. Metal ion catalysis: metal ions gain or lose electrons without detaching from enzymes. Meaning, that depends on tertiary structure of the enzyme: hydrogen bonds, attraction/repulsion of electric-charged groups, hydrophobic interactions. Enzyme changes shape when it binds a substrate. This type of shape change is called induced fit altering the shape of the active site of the enzyme. Provides framework so that amino acids can be properly positioned. Some enzymes require other molecules in order to function.
