1. The initial reaction rate (V0) of any enzyme following Michaelis–Mentenkinetics is 50% of Vmax. In this case, find th
Posted: Thu Jun 09, 2022 6:14 am
1. The initial reaction rate (V0) of any enzyme following
Michaelis–Mentenkinetics is 50% of Vmax. In this case, find the
ratio ([S]: KM value) between [S] and KM, and briefly describe the
calculation process.
2. List three amino acids that can be phosphorylated by
Kinase.
3. Briefly describe Enzyme's definition of competitive
inhibitor and provide two examples of competitive inhibitor.
(Describe the name of the inhibitor and the type of target protein
briefly)
4. Based on the figure below, predict what peptide bond
could be the substrate of each protease
(The bond marked in blue is where hydrolysis occurs, choose 2
peptides per protease type)
Chymotrypsin:_________ Trypsin:_________ Elastase:_________
1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SG
Thanks in advance!!
v Chymotrypsin Asp 189 Asp 189 Trypsin Val 190 Val 216 wake Val 216 Elastase Val 190
Michaelis–Mentenkinetics is 50% of Vmax. In this case, find the
ratio ([S]: KM value) between [S] and KM, and briefly describe the
calculation process.
2. List three amino acids that can be phosphorylated by
Kinase.
3. Briefly describe Enzyme's definition of competitive
inhibitor and provide two examples of competitive inhibitor.
(Describe the name of the inhibitor and the type of target protein
briefly)
4. Based on the figure below, predict what peptide bond
could be the substrate of each protease
(The bond marked in blue is where hydrolysis occurs, choose 2
peptides per protease type)
Chymotrypsin:_________ Trypsin:_________ Elastase:_________
1. SR−SG 2. SF−SG 3. SK−SG 4. SA−SG 5. SV−SG 6. SM−SG
- 1 The Initial Reaction Rate V0 Of Any Enzyme Following Michaelis Mentenkinetics Is 50 Of Vmax In This Case Find Th 1 (182.18 KiB) Viewed 41 times
v Chymotrypsin Asp 189 Asp 189 Trypsin Val 190 Val 216 wake Val 216 Elastase Val 190