1.Serine protease is one of the most studied mechanisms in biochemistry. Step 1: H+ shift generates Ser-O Step 5: C-Terminal peptide leaves His His Ser NEHO Asp Asp NH2 C-Termı Bulky Side Chain Buiky Side Chain C-Terminus NI N-Term N-Term Step 2: Ser-O binds to C=O Step 6: ionization of water His His Asp -C Asp - Buiky Side Chain Buiky Side Chain C-Termn N-Term N-Term Step 3: Transition State I Step 7: Transition State II His His Asp -C Ser Asp -C Şer N- -- Bulky Side Chain C- BuIky ! Side Chain C-Term N-Term N-Term Step 4: Peptide bond breaks Step 8: N-terminal peptide leaves His His Ser Ser но Asp DH =N C-Term Bulky Side Chain New Substrate - Bulky Side Chain o-5. N-Term NH N-Terminus a. Using the diagram provided, discuss the key feature of the mechanism. b. Not shown in this diagram, there is a hydrophobic pocket on the enzyme. Why does it have a hydrophobic pocket? What effect would there be if in the active site histidine were replaced with lysine? Explain. C.
Catalysis and Enzymatic Reactions
Catalysis is the kind of chemical reaction in which the rate (speed) of a reaction is enhanced by the catalyst which is not consumed during the process of reaction and afterward it is removed when the catalyst is not used to make up the impurity in the product. The enzymatic reaction is the reaction that is catalyzed via enzymes.
Lock And Key Model
The lock-and-key model is used to describe the catalytic enzyme activity, based on the interaction between enzyme and substrate. This model considers the lock as an enzyme and the key as a substrate to explain this model. The concept of how a unique distinct key only can have the access to open a particular lock resembles how the specific substrate can only fit into the particular active site of the enzyme. This is significant in understanding the intermolecular interaction between proteins and plays a vital role in drug interaction.
1.Serine protease is one of the most studied mechanisms in biochemistry.
A. Using the diagram provided, discuss the key feature of the mechanism.
B. Not shown in this diagram, there is a hydrophobic pocket on the enzyme. Why does it have a hydrophobic pocket?
C. What effect would there be if in the active site histidine were replaced with lysine? Explain.
Please refer to photo for the diagram
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