Enzymes I+II- Lecture 8/31/21 Flashcards
(42 cards)
Elastase
A protease that destroys elastin, which destroys the lining of the lungs
How can enzyme activity be deficient
Enzyme isn’t made
Enzyme is made but has a mutation that lowers activity
Insufficient substrate
inhibited
Catalyst
Third party that alters the kinetics of a reaction without being altered itself
Oxidoreductases
Catalyze an oxidation-reduction rxn, ex: NAD+->NADH
Transeferases
Transfer of a chemical group ex: kinases
Hydrolases
Lysis of water, ex: protease
Lyases
A cleavage rxn not using water
Isomerases
Change of a molecular configuration
Ligases
Joining of two compounds ex: DNA poly
Delta G
Change in free energy
Spontaneous rxn
Has a negative delta G
Gibbs free energy equations
DeltaG=DH-TDS
Standard conditions for DGo
Certain temp, 1 M conc, except [H+] is pH of 7
Gibbs free energy in not standard conditions
DG=DGo+RTlnQ
Q
Q= [Products]/[reactants]
Equilibrium
When DG=0
Keq
Q at equilibrium
Keq=e>-DGo/RT
When Q>Keq
The reaction goes in reverse
When Q
Reaction proceeds forward, removal of product drives reaction forward
Transition state
High energy intermediate, stabilization by catalyst allows for the activation energy to be lowered and the rxn to proceed faster
Catabolism
The breakdown of energy yielding nutrients to gain energy in the form of ATP, NADH
Anabolism
Using simple precursor molecules to build complex molecules needed for life, includes active transport and mechanical work
Multibinding enzymes
Enzymes can bind more than one substrate, and often couple an exergonic rxn with an endergonic one
Serine proteases
Proteolytic enzymes that catalyze peptide bond hydrolysis by using activated serine resides to add water and break the bond