1Define catalyst.
a substance that can increases the rate of chemical reaction
2State the role of enzymes in the chemical reactions on which life is based.
Enzymes are biological catalysts, they speed up biochemicals reactions to occur quickly enough to sustain life processes.
3state that enzymes speed up chemical reactions without being altered, so can be reused.
Enzymes are not consumed in the reaction and can catalyze additional reactions.
4Define metabolism.
The sum of all chemical reactions taking place in a cell at one time.
5Define specificity in relation to enzyme structure and function.
only 1 substrate will fit in the active site of an enzyme
This prevents unwanted side reactions and allows precise regulation of metabolic pathways.
6Outline how control of metabolism is regulated by enzymes.
If a cell produces an enzyme it can increase the speed of reaction that would otherwise happen slowly
7Contrast anabolic and catabolic reactions.ate that enzymes speed up chemical reactions without being altered, so can be reused.
Anabolic reactions synethise simple moleclues into complex molecules and catabolic reactions breakdown the complex molecules into simple molecules
Anabolic reactions require energy input, while catabolic reactions release energy.
8List three examples of anabolic processes
photosynthesis protein synthesis and DNA replication
9List three examples of catabolic processes.
glycosis, digestion and cellular respiration
10Outline properties of globular proteins.
3d structure made out of amino acids. The amino acids that make up the activiation site may not be next to eachother in the polypeptide chain but are brought together by polypeptide folds(creates the 3d protein)
11Explain the relationship between enzyme structure and enzyme specificity, including the structure and function of the active site.
Enzyme specificity is determined by the shape of its active site, which only fits specific substrate molecules.
The active site binds to the substrate through interactions like hydrogen bonding or van der Waals forces, facilitating a chemical reaction and ensuring the enzyme catalyzes only specific reactions.
12Outline the stages of enzyme catalysis of a chemical reaction.
1) substrate goes into the active site of an enzyme through lock and key or induced fit(enzyme-substrate complex)
2)anabolic or catabolic reaction occur(This stresses substrate bonds, lowering activation energy)
3)products are released from active site
13Describe the induced fit model of enzyme binding.
Substrate specific but not a fixed shape
1-Substrate binds to active site
2-Active site changes shape (conformational change)
3-Affects bonding in substrate(This stresses substrate bonds, lowering activation energy)
4-Product releases
5-Active site returns to original shape
14Explain the role of random collisions(collision thoery) in the binding of the substrate with the enzyme active site.
Chemical reactions require molecules to collide.
They must have enough energy and the right orientation when they collide. Collisions can be increased by increasing temperature and concentration
15Compare enzyme and substrate movement involved in reactions that occur in the cytoplasm, with large substrates and with immobilized enzymes.
In cytoplasmic reactions, both enzymes and substrates are free to move and randomly collide, facilitating interactions.
With large substrates, their slower movement may limit interaction rates, while immobilized enzymes remain fixed in place, requiring substrates to move towards them for the reaction to occur.
16Discuss variation in specificity of different enzymes.
-Some enzymes can only bind with one substrate
-Other enzymes can bind with several closely related substrated
17Define denaturation
permanent change to the 3d structure of the active site of an enzyme causing the enzyme to be unable to catalyze the reaction
18Outline the causes and effects of denaturation on enzyme structure and function.
Causes:
Temp(When enzymes heated, bonds vibrate and are more likely to break)
pH(acditiy) If pH increases or decreases from the optimum, ionic bonds between amino acids in enzymes are altered and denatured
19Outline the effects of denaturation on enzyme structure and function.
Effects to active site: prevent binding of substrates, prevent catalysis after binding
20Explain the effects substrate concentration on enzyme structure and function with reference to collision theory.
As concentration increases more frequent collisions occurr. Past a certain point the slope stagnates as all active sites are occupied
21Draw and interpret graphs showing the effects of temperature, pH and substrate concentration of the activity of enzymes.
draw Slides 5 to 7
22Identify the manipulated (independent), responding (dependent) and controlled variation in experiments of enzyme catalyzed reactions.
The factor being investigated ( manipulated )
temperature substrate concentration, enzyme concentration or pH
23State the unit for enzyme reaction rate.
Amount of reaction / per unit time
24State two methods for determining the rate of enzyme reaction rates.
1. Allow reaction to happen for a set amount of time and measure the amount of substrate used or product
2. Start with known amount of substrate and measure time taken for all substrates to convert to products
25Define activation energy.
Energy needed to get a reaction started. It is used to break or weaken bonds in the substrate
26State that activation energy is used to break or weaken bonds in the substrate.
an amount of energy is needed to Break bonds in substrate molecules to form products
27Explain the role of enzymes in lowering the activation energy of a reaction.
Enzymes speed up reactions by lowering the activation energy by providing reactants an alternative pathway.