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This chapter from 'biochemistry: a short course' explores the role and mechanisms of enzymes as powerful catalysts in biological systems. Topics include the specificity of enzymes, cofactors, and the thermodynamics of enzyme-catalyzed reactions. Key concepts include the interaction between enzymes and substrates, the importance of the active site, and the role of transition state analogs as inhibitors.
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Basic Concepts of Enzyme Action
Enzymes are powerful and highly specific catalysts Accelerate reaction Most reactions in biological systems do not take place in the absence of enzymes
Carbonic anhydrase – fastest enzymes known It adding water to carbondioxide – simple reaction Transfer of corbon dioxide from the tissues to the blood They are highly specific Catalyzes a single reaction or a set of closely related reaction
carboxyl side of lysine and arginine residues Thrombin- catalyzes the hydrolysis of Arg-Gly bonds
The specificity of an enzyme is due to the precise interaction of the substrate with the enzyme. This precision is a result of the intricate three- dimensional structure of the enzyme protein.
Free energy is useful thermodynamic function for understanding enzymes Thermodynamic properties of a reaction depends on
1.The active site takes up a small part of the total volume of an enzyme.
The active site of the unbound enzyme is complementary in shape to the substrate – lock and key