Chat with us, powered by LiveChat Question: D) In The Proposed Mechanism Of The Phytase Enzyme, The Catalytic His17 Performs A Nucleophilic Attack On The Nearby Phosphate Moiety, Resulting In Transfer Of The Phosphate From Phytate To His17. The Histidine-phosphate Linkage Is Then Broken By Hydrolysis In The Second Step, Perhaps Catalyzed By The Same Acid-base ("B") As Used In Step 1. Step 1 I ... | Wridemy

17 Aug Question: D) In The Proposed Mechanism Of The Phytase Enzyme, The Catalytic His17 Performs A Nucleophilic Attack On The Nearby Phosphate Moiety, Resulting In Transfer Of The Phosphate From Phytate To His17. The Histidine-phosphate Linkage Is Then Broken By Hydrolysis In The Second Step, Perhaps Catalyzed By The Same Acid-base (“B”) As Used In Step 1. Step 1 I …

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d) In the proposed mechanism of the phytase enzyme, the catalytic His17 performs a nucleophilic attack on the nearby phosphate moiety, resulting in transfer of the phosphate from phytate to His17. The histidine-phosphate linkage is then broken by hydrolysis in the second step, perhaps catalyzed by the same acid-base (“B”) as used in Step 1. Step 1 I O B-H O Step 2 B-H O Pi O Pi a. In the 3BPH structure, which phosphate would be in position to be removed first (if the enzyme were not dead)? Identify it by the number of the carbon on the inositol ring (i.e., 1, 2, 3. 4. 5, or 6) b. Which residue do you think could play the role of the aci Љase in the mechanism? (If you think that are 2 candidates, and you think that they are more or less equally likely to play this role, you can mention both.) +3

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