Back to AI Flashcard MakerBiology /Chapter 6: An Introduction to Metabolism Part 2
Chapter 6: An Introduction to Metabolism Part 2
This flashcard deck covers key concepts from Chapter 6, focusing on metabolism, enzyme function, and reaction dynamics. It includes questions and answers on ATP regeneration, enzyme mechanisms, and factors affecting reaction rates.
Where does the energy required for the regeneration of ATP come from?
exergonic (catabolic) reactions in the cell
Tap or swipe ↕ to flip
Swipe ←→Navigate
1/33
Key Terms
Term
Definition
Where does the energy required for the regeneration of ATP come from?
exergonic (catabolic) reactions in the cell
What is ATP converted into?
ADP and phosphate, which are more stable
What does the loss of a phosphate do?
makes ADP have less NRG and be more stable
Is the regeneration of ATP an exergonic or endergonic reaction?
endergonic
Is the breaking of ATP an exergonic or endergonic reaction?
exergonic
What is the rate of reaction?
the speed at which a reaction moves toward equilibrium, which is controlled by concentration gradients and enzymes
Related Flashcard Decks
Study Tips
- Press F to enter focus mode for distraction-free studying
- Review cards regularly to improve retention
- Try to recall the answer before flipping the card
- Share this deck with friends to study together
| Term | Definition |
|---|---|
Where does the energy required for the regeneration of ATP come from? | exergonic (catabolic) reactions in the cell |
What is ATP converted into? | ADP and phosphate, which are more stable |
What does the loss of a phosphate do? | makes ADP have less NRG and be more stable |
Is the regeneration of ATP an exergonic or endergonic reaction? | endergonic |
Is the breaking of ATP an exergonic or endergonic reaction? | exergonic |
What is the rate of reaction? | the speed at which a reaction moves toward equilibrium, which is controlled by concentration gradients and enzymes |
What is an enzyme? | a macromolecule that acts as a catalyst to speed up a reaction without being consumed by the reaction |
What is the activation energy? | the initial investment of energy necessary to break bonds in the reactants and get the reaction started |
What is activation energy often in the form of? | heat that the reactant molecules absorb from the surroundings |
What does the activation energy, when inputted, do? | allows the reactants to reach their transition state at which point they are unstable and primed to break and reform bonds |
Why is adding heat, even though it speeds up a reaction, not appropriate for most biological systems? | high temperatures denatures proteins and kills cells and it would speed up all reactions, not just the one needed |
How does an enzyme catalyze a reaciton? | by lowering the activation energy needed enabling the reactant molecules to absorb enough energy to reach the transition state at moderate temperatures |
What is a substrate? | the reactant that an enzyme acts on |
What is the enzyme-substrate complex? | the enzyme binds to its substrate |
What part of an ennzyme actually binds with the substrate? | the active site |
What is the specificity of an enzyme attributed to? | the compatible fit between the active site and the substrate |
Explain the concept of induced fit. | The active site does not fit rigidly like a lock and key. As the substrate enters the active site interaction of the R groups of the amino acids causes the enzyme to change its shape slightly so that the active site fits even more snuggly around the substrate |
T/F: Enzymes are anabolic | False - (kind of) Enzymes can be catabolic or anabolic depending on whether they break down or combine molecules respectively |
What are the four enzyme mechanisms that lower activation energy? | 1.) The active site provides a template for the substrates to come together.
2.) The enzyme stresses and bends the chemical bonds that must be broken thus lowering activation energy.
3.) The active site provides a microenviroment that is conductive for the reaction to proceed.
4.) Direct participation of the active site in the chemcial reaction |
What are the factors that affect the rate of reaction? | Substrate concentration, enzyme concentration, temperature, and pH |
Explain how substrate concentration affects the rate of reaction? | Increasing substrate concentraition will increase the rate of reaction in direct proportion until all enzume molecules have their active site engaged. At that point the enzyme is said to be saturated. The only way then to increase the rate of reaction is to increase the amount of enzyme. |
Explain how enzyme concentration affects the rate of reaction? | Increasing the enzume concentration will increase the rate of reacition as long as there is enough substrate for enzymes to work on. |
Explain how temperature affects rate of reaction. | Enzyme rate will increase until a point where the enzyme denatures |
Explain how pH affects rate of reaction. | Most work best at a pH of 7 but will vary depending on the enzyme |
What are coenzymes? | organic molecules that aid enzymes in lowering activation energy. Many of these are vitamins that we get in our diet. |
What are cofactors? | inorganic enzyme helpers, which are usually minerals. |
What determines if an inhibitor is reversible or irreversible? | if an inhibitor attaches to the enzyme by a covalent bond it is usually irreversible but if it attaches by weak interactions the inhibition is reversible |
What do competitive inhibitors do? | reduce the productivitiy of enzymes by blocking substrates from entering the active site. This type of inhibition can be reversed by increasing the concentration of the original substrate. |
What do noncompetitive or allosteric inhibitors do? | do not directly compete with the substrate for active sites. Instead they bind to another part of the enzyme changing the enzyme's shape so that it is less effective. The site of attachment is called the allosteric site. |
What is allosteric regulation? | the term used to describe any case in which a protein's function at one site is affected by the binding of a regulatory molecule to a seperate site. |
What can allosteric regulation result in? | either activation or inhibition |
What happens in cooperativity? | the binding of one substrate molecule can stimulate the binding or activity at other active sites. |
What happens in feedback inhibition? | the end product of a metabolic pathway allosterically inhibits the enzyme from a previous step in the pathway. Most commonly used to maintain homeostasis by preventing overproduction of products in a cell (negative feedback). |