MBB 222 Lecture Notes - Lecture 7: Adenylate Kinase, Enzyme Catalysis, Hydrolysis
20 Dec 2018
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Document Summary
Enzymes may convert energy from one form into another. In many biochemical reactions, the energy of the reactants is converted with high efficiency into a different form. Example: photosynthesis light energy is converted into chemical-bond energy. Ca2+-atpase catalyzes the hydrolysis of atp and uses the energy from this reaction to transport ca2+ across the membrane, generating a ca2+ gradient. The active sites of enzymes have some common features. The active site is usually a cleft or crevice formed by the three-dimensional structure of the folded enzyme - functional groups that come from different amino acids in the active site participate in catalysis. The active site takes up a relatively small part of the total volume of an enzyme. Substrates associate with enzymes via multiple weak interactions (recall noncovalent bonds). Example of an induced-fit mechanism for the binding of a substrate analog to e. coli adenylate kinase.
