Dr Quan Exam 1 Study Guide Flashcards
Most critical function of an enzyme
Accelerate reactions by millions fold
Optimum temperature for enzymes
37 degrees C
Optimum pH for enzymes
~7
Pepsin exception: 1.5-2
Composition of complex enzyme
Apoenzyme (protein part) and Cofactor (Prosthetic group or Coenzyme)
Catalyze oxidation-reduction reactions
Oxidoreductase
Catalyzes group transfers
Transferase
Catalyzes hydrolysis rxns where water is acceptor of transferred group
Hydrolase
Catalyze isomerization rxns (D to L, L to D)
Isomerase
Catalyze the lysis of substrate, generating a double bond in a nonhydrolytic, nonoxidative elimination.
Lyases
Catalyze joining of two substrates and requires ATP (energy)
Ligase
Specific region of enzyme where substrate molecule is bound
Active Site
Enzyme active site only able to accept specific substrate type
Lock and Key Theory (Fischer Theory)
Enzyme acts only on one substrate
Absolute Specificity
Enzyme acts on different substrates that have same bond type
Relative Specificity
Enzyme Activity Definition
1 international unit (IU) of enzyme catalyzes conversion of 1 micromol of substrate to product per minute
Km (Michaelis Constant) definition
Substrate concentration @ 1/2 Vmax
Reversible Inhibitors
Can rapidly dissociate
Weak, noncovalent interaction
Irreversible Enzyme Inhibition
Slow dissociation of EI complex
Tightly bound
Competitive Inhibitor
Competes with substrate at active site.
Km increased, Vmax unchanged
Non-competitive inhibitor
Binds to enzyme site different from active site.
Km unchanged, Vmax decreased
Uncompetitive Inhibitors
Binds to ES complex (not free enzyme)
Decreases both Km and Vmax