Chapter 8: Energy and Enzymes Flashcards
Energetic coupling
Basically mechanisms from gen chem 2. A very spontaneous reaction is coupled with a non-spontaneous reaction so that the non-spontaneous reaction can actually happen. Many non-spontaneous reactions are critical to life, therefore energetic coupling is essential to life.
How do enzyme activation sites reduce activation energy?
Enzymes bring reactants together in precise orientations, making reactions more likely to happen
How does temperature affect enzymes?
Enzymes are proteins, and being at the wrong temperature will cause an enzyme to fold improperly and therefore become denatured and ineffective
How does pH affect enzyme effectiveness?
pH affects an enzyme’s shape and reactivity and will affect the charge of acidic and basic groups, which will also denature the enzyme and make it become ineffective
Competitive inhibition
A similarly shaped substrate (competitive inhibitor) will bind to an enzyme’s active site and prevent the enzyme’s action due to the competitive inhibitor not actually being the substrate.
Allosteric regulation
A regulatory molecule changes the shape of the enzyme which will either activate the enzyme or inhibit its action by attaching to somewhere on the enzyme that isn’t the active site
Describe the structure of monosaccharides
Differ in whether the molecule contains a ketone group or an aldehyde group
Arrangement of hydroxyl groups
Ring structure (ex. 5 carbon sugar forms pentagon)
Glycosidic linkages between monomers
Bonding between alcohol groups of monomers
Substrates are what?
What binds to an enzymes activation site
Allosteric Regulation
Something binds to somewhere on an enzyme that is not the activation site, and this will change the shape of the protein. This can either deactivate or activate an enzyme (allosteric inhibition and allosteric activation) respectively
Phosphorylation of Enzymes
Chemically change the enzyme to either activate or deactivate it
