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23 Cards in this Set

  • Front
  • Back
Two important points about how enzymes support life.
(1)they efficiently accelerate chemical reactions
(2) with a high degree of specificity
Define cofactor.
inorganic ions (trace nutrients, vitamins, metals) that are required by some enzymes for their catalytic activity.
Define coenzyme.
complex organic or metallo-organic molecules that are required by some enzymes for their catalytic activity
Define prosthetic group.
A coenzyme or metal ion that is very tightly or even covalently bound to the enzyme protein
Define holoenzyme.
the complete, catalytically active enzyme complex together with its bound coenzyme and/or metal ions.
Define apoenzyme/apoprotein.
the protein part of the enzyme without cofactors or prosthetic groups. It is catalytically inactive.
define active site.
area on an enzyme containing the amino acid side chains that are involved in catalyzing the reaction.
Define substrate.
The molecule that is bound in the active site and is acted on by the enzyme to form the product.
What do the oxidoreductases do?
Transfer electrons (hydride ions or H atoms)
What do transferases do?
They group transfer reactions.
What do hydrolases do?
They hydrolyze reactions (transfer functional groups to water)
What do lyases do?
The add groups to double bonds or form double bonds by removal of groups
What do isomerases do?
They transfer groups within molecules to yield isomeric forms.
What do ligases do?
They form C-C, C-S, C-O, and C-N bonds by condensation reactions coupled to ATP cleavage.
Bottom line with enzymes (three big points).
(1) high degree of specificity
(2) enzymes are proteins (with few exceptions)
(3) enzymes are classified according to the type of reaction that they catalyze
Name two distinguishing features of an enzyme-catalyzed reaction.
(1) the reaction only takes place within the confines of a pocket called the ACTIVE SITE.
(2) The molecule bound selectively to the active site and acted upon by the enzyme is called a SUBSTRATE.
T/F: enzymes affect the position and direction of equilibrium.
false.
What controls the speed of reaction?
The reaction energy path controls the reaction speed.
Name two ways rate of reactions can be increased.
(1) raising the temperature, thereby increasing the number of molecules with sufficient energy to overcome the energy barrier
(2) lowering the activation energy: adding an enzyme.
What is the 'rate-limiting step'?
When several steps occur in a reaction, the overall rate is determined by the step with the highest activation energy. This step is the rate-limiting step. It limits the throughput of the reaction.
What are enzyme inhibitors?
Molecular agents that interfere with catalysts, slowing or halting enzymatic reactions.
what is the relationship between the activation energy and the rate of reaction?
a higher activation energy corresponds to a slower reaction
how do enzymes decrease activation energy?
Enzymes decrease the activation energy by forming enzyme-substrate (ES) complexes and enzyme-product (EP) complexes). It accelerates the interconversion of S and P; this is a bidirectional catalyzing reaction. The reaction reaches the equilibrium point must faster, but the final equilibrium point is unaffected.