Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
16 Cards in this Set
- Front
- Back
Activation Energy (Ea)
|
the initial investment of energy for starting a reaction;
the energy required to break the bonds of the reactants |
|
Catalysts
|
chemical agents that speed the rate of a chemical reaction without being consumed or changed
|
|
How are catalysts thought to work?
|
By lowering the activation energy needed for a reaction to occur.
|
|
Most catalysts in organisms are made up of what?
|
Enzymes (proteins)
|
|
What is ribozyme?
|
RNA acting as a catalyst for a few biochemical reactions
|
|
Structure of Enzymes:
|
Globular proteins.
Simple or conjugated. |
|
Depending on the relative concentration of reactants and products, Enzymes can...
|
...catalyze a reaction in either direction.
It does not determine the direction |
|
What are substrates?
|
Reactants in enzyme catalyzed reactions
|
|
Enzymes differ in _____?
|
specificity
|
|
2 specificities of enzymes and corresponding meaning
|
Very specific- only catalyze one specific type of reaction. (eg urease)
Non-specific -- will catalyze several different, but very similar reactions (eg lipase) |
|
Enzymes work primarily based on their _____?
|
3D shape, which is distinctive for each type of enzyme.
|
|
What is the active site of an enzyme?
|
Portion of an enzyme that interacts with a substrate
|
|
2 theories of active site and substrate fit, and their differences?
|
Lock and Key model- enzyme won't change shape.
Induced-fit model (most common) - Enzyme changes shape temporarily |
|
3 ways enzymes may help speed up a reaction
|
Bringing substrates close together.
Orient substrates correctly for reaction. Weaken bonds in substrate so they will break. |
|
3 Environmental factors that affect enzyme reaction rate
|
Temperature
pH Inhibition |
|
2 types of Inhibitors and their meaning
|
Competitive - very similar in structure to the normal substrate; they compete with the normal substrate for binding to the active site.
Non-competitive -- do not resemble the structure of the normal substrate; bind to the allosteric site and change the shape of the enzyme and its active site |