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16 Cards in this Set
- Front
- Back
- 3rd side (hint)
Define Enzymes (6) |
1. Biological catalysts 2. made up of proteins 3. that lower the activation energy required 4. for a chemical reaction to occur, 5. speeding up the rate of chemical reactions 6. without themselves being chemically changed at the end |
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Why Enzymes are needed: (4) |
1. Food stains (Proteins, Carbohydrates, Fats) molecules too big 2. Insoluble in water 3. Enzymes digest nutrients in food to 3S S. mall S. oluble S. imple 4. So that they can pass through the cell membrane |
Stains = P. ro C. arry F. iora |
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Define Catalysts (2) |
1. substance that alters/speeds up the rate of chemical reactions 2. Without being chemically changed at the end |
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Define Activation Energy |
The energy needed to start a chemical reaction. |
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Digestive Enzymes (4) |
1. Amylase - Starch > Maltose > 2. Maltase - Maltose > Glucose 3. Pepsin - Protein > Polypeptide 4. Lipase - Fats > Glycerol + 3 Fatty Acids |
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Define Anabolic Reactions + One Example |
Building Up Reactions Eg. 1. Amino Acids > Polypeptide (chains) 2. Fatty Acids + glycerol > Fats 3. Glucose > Starch/Glycogen |
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Define Catabolic Reactions + One Example |
Breaking Down Reactions Eg. Breaking down of Glucose during respiration 1. Digestion of Food Substances 2. Starch > Glucose 3. Glucose > Oxygen (Cellular Respiration) |
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Define Hydrolases |
Enzymes that catalyze Hydrolytic Reactions |
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Characteristics of Enzymes (3) |
1. Speed up chemical reactions 2. Only required in minute amounts 3. Highly specific in action (Due to its 3D shape) |
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Lock & Key Hypothesis (6) |
1. Reactions depends on active site. (Enzyme specific 3D shape, active site present) 2. Only Substrate w/ 3D shape complementary to active site can bind & FIT into the enzyme 3. to form enzyme-substrate complex 4. substrate > products 5. Products detach from active site 6. enzyme chemically unchanged (can be reused again) |
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Define Denaturation (4) |
1. The change in 3D shape 2. of an enzyme or any protein 3. caused by extremely High Temp. 4. or extreme pH. |
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What happens when an enzyme is denatured (6) |
1. Weak Hydrogen Bonds are broken. 2. Loss of 3D structure & active site. 3. Cannot bind with substrate. 4. No enzyme-substrate complex formed. 5. No reaction takes place. 6. No product is formed. |
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Affected By Temperature (graph desc. in 4 parts) |
A: Low Temp: Enzymes are inactive. Very Low: 1. K.E. 2. Chances of substrate molecules colliding with enzymes. B: Temp increases As the temp. ^, Increases: - Enzyme activity - K.E. of molecules - Rate of collision between substrate & enzyme - Rate of formation of enzyme-substrate complex C: Optimum Temp. "point where rate of reaction is highest, where enzymes are most active" D: Beyond C, - enzyme activity decreases - HIGH temp BREAKS the weak Hydrogen bonds within the enzyme, changes its 3D shape - Active site loses its 3D shape - Denatured |
Divide the graph into 4 parts |
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Affected by pH |
Extreme changes denature enzyme, cause it to lose function - Some proteins extreme pH Eg: Pepsin in stomach, pH 2-3 |
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Amino Acid Structure: |
H H O l l ll H - N - C - C - OH l R |
Amino Group ( H - N ^l H ) Side Chain (R) Carboxylic Acid Group |
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Define Catalase (2) |
- Enzyme that catalyzes breakdown of Hydrogen Peroxide - Into H20 + O2 |
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