Biochemistry
Enzyme Catalytic Strategies
Compiled By Simon Mwangi
Edition: 2024/25
, Science | Biochemistry I of V pages
1. 2 things that enzyme activity depend on?
pHTemperature
2. How does increase in temp affect enzyme activity?
Increases it as molecules move faster
3. 4 catalytic principles used by enzymes
Covalent catalysisGeneral acid-base catalysisCatalysis by approximation Metal ion catalysis
4. Which catalytic strategies does chymotrypsin combine?
Covalent, acid-base and transition-state
5. What does protease catalyse?
ProteolysisCuts down proteins
6. Difference between nucleophile and electrophile
Nucleophile: Accepts protons and donates electronsElectrophile: Donates protons and accept electrons
7. What is chymotrypsin involved in?
Breaking down proteins into small peptides by cutting a specific location on peptide backbone
8. What is the catalytic triad?
Serine, Histadine and AsperegineThey have to be close in the folding
9. Where does the cutting occur in chymotrypsin?
In the hydrophobic pocket, the serine cuts the protein when it is attached to the hydrophobic pocket
10. What does the oxyanion hole do?
Protects the enzyme
11. Does the S1/hydrophobic pocket differ in protease?
Yes
12. Do proteases cut in only one point?
Yes
13. What allows for the specificity in proteases?
The difference in hydrophobic pockets
14. Example of aspartyl protease
Pepsine
15. What is site-directed mutagenesis?
Replace one amino acid with anotherExample how the catalytic triad was discovered
16. 3 classes of proteases
CysteineAspartylMetalloproteases
Biochemistry 2024/25 Edition
Enzyme Catalytic Strategies
Compiled By Simon Mwangi
Edition: 2024/25
, Science | Biochemistry I of V pages
1. 2 things that enzyme activity depend on?
pHTemperature
2. How does increase in temp affect enzyme activity?
Increases it as molecules move faster
3. 4 catalytic principles used by enzymes
Covalent catalysisGeneral acid-base catalysisCatalysis by approximation Metal ion catalysis
4. Which catalytic strategies does chymotrypsin combine?
Covalent, acid-base and transition-state
5. What does protease catalyse?
ProteolysisCuts down proteins
6. Difference between nucleophile and electrophile
Nucleophile: Accepts protons and donates electronsElectrophile: Donates protons and accept electrons
7. What is chymotrypsin involved in?
Breaking down proteins into small peptides by cutting a specific location on peptide backbone
8. What is the catalytic triad?
Serine, Histadine and AsperegineThey have to be close in the folding
9. Where does the cutting occur in chymotrypsin?
In the hydrophobic pocket, the serine cuts the protein when it is attached to the hydrophobic pocket
10. What does the oxyanion hole do?
Protects the enzyme
11. Does the S1/hydrophobic pocket differ in protease?
Yes
12. Do proteases cut in only one point?
Yes
13. What allows for the specificity in proteases?
The difference in hydrophobic pockets
14. Example of aspartyl protease
Pepsine
15. What is site-directed mutagenesis?
Replace one amino acid with anotherExample how the catalytic triad was discovered
16. 3 classes of proteases
CysteineAspartylMetalloproteases
Biochemistry 2024/25 Edition
