Chapter 8 Flashcards
(13 cards)
Exergonic
has a RELEASE of free energy to the surroundings
Occurs spontaneously since they do not require energy to start
Endergonic reaction
ABSORBS free energy from the surroundings
Metabolism
Set of chemical reactions that converts molecules into other molecules while transferring energy.
Metabolism - Two branches
Catabolism - Breaks down molecules into smaller units. Produces ATP, ADP, and P
Anabolism - Builds molecules from smaller units. Requires energy in the form of ATP hydrolyzed to ADP or P.
3 common types of cell energy
1.ATP
2.ADP
3.AMP
All three hold chemicals in their bonds.
Structure and Hydrolysis of ATP
ATP (adenosine triphosphate) is composed of Ribose, Adenine,
Enzymes - Metabolic Catalyst
-A catalyst is a chemical agent that speeds up a reaction without being consumed by the reaction
-An enzyme is a protein that acts as a catalyst to speed up a specific reaction
Substrate Specificity of Enzymes
1.The reactant that an enzyme acts on is the enzyme’s substrate
2.The active site is the region on the enzyme, that binds to the substrate
3.The enzyme binds to its substrate, forming an enzyme-substrate complex.
Enzymes and Temperature/pH(5 things)
1.Enzymes have an optimal temperature and pH
2.At low temps, reactions happen slowly because low kinetic energy
3.At high temps faster movement and molecules means more reactions up to a point
4.When enzymes get too hot, they denature
5.Enzymes are suited for pH according to their type
Denature
When enzyme structure breaks down
Cofactors
1.Many enzymes require non-protein helpers for catalytic and activity
2.Cofactors are non-protein helpers that bind to the enzyme permanently, or reversibly with substrate
-Inorganic cofactors include metal atoms such as zinc, iron, and copper
-Organic cofactors are called coenzymes
Inhibitors- decrease the activity of enzymes
Reversible inhibitors
-Form weak bonds with enzymes
Irreversible inhibitors
-Form covalent bonds with enzymes
2 types of methods to inhibit
1.Competitive inhibitors bind to the active site, blocking substrate from binding.
2.Non-competitive inhibitors bind to allosteric site and change shape of enzyme, preventing production of product (Allosteric inhibitors)
3.Cells use Allosteric inhibitors to stop or move on to the next step in a metabolic pathway