1. What is the best description of the \"oxyanion hole\" generated during the me
ID: 151826 • Letter: 1
Question
1. What is the best description of the "oxyanion hole" generated during the mechanism of a serine protease - catalyzed reaction? a. the oxyanion hole is generated as a result of deprotonation of the serine by a neighboring histidine, resulting in a negatively charged oxygen nucleophile b. the oxyanion hole describes the binding pocket for the phenylalanine amino acids that are preferred substrates for the serine proteases c. the oxyanion hole describes the stabilization of the tetrahedral intermediate where H-bonding lowers the energy of the negatively charged oxygen resulting from nucleophilic attack on the carbonyl carbon. d. the oxyanion hole describes the planar enzyme-substrate intermediate formed as the carbonyl double-bond is reformed.2.Which statement describes a common feature of both the RNase A and Serine Protease mechanisms? a.A deprotonated serine acts as a nucleophile b. a covalent enzyme-substrate intermediate is formed c. Water is protonated by a Histidine to generate an acidic hydronium ion. d. a Histidine acts as a Bronsted base to remove a proton from an alcohol group. 1. What is the best description of the "oxyanion hole" generated during the mechanism of a serine protease - catalyzed reaction? a. the oxyanion hole is generated as a result of deprotonation of the serine by a neighboring histidine, resulting in a negatively charged oxygen nucleophile b. the oxyanion hole describes the binding pocket for the phenylalanine amino acids that are preferred substrates for the serine proteases c. the oxyanion hole describes the stabilization of the tetrahedral intermediate where H-bonding lowers the energy of the negatively charged oxygen resulting from nucleophilic attack on the carbonyl carbon. d. the oxyanion hole describes the planar enzyme-substrate intermediate formed as the carbonyl double-bond is reformed.
2.Which statement describes a common feature of both the RNase A and Serine Protease mechanisms? a.A deprotonated serine acts as a nucleophile b. a covalent enzyme-substrate intermediate is formed c. Water is protonated by a Histidine to generate an acidic hydronium ion. d. a Histidine acts as a Bronsted base to remove a proton from an alcohol group. a. the oxyanion hole is generated as a result of deprotonation of the serine by a neighboring histidine, resulting in a negatively charged oxygen nucleophile b. the oxyanion hole describes the binding pocket for the phenylalanine amino acids that are preferred substrates for the serine proteases c. the oxyanion hole describes the stabilization of the tetrahedral intermediate where H-bonding lowers the energy of the negatively charged oxygen resulting from nucleophilic attack on the carbonyl carbon. d. the oxyanion hole describes the planar enzyme-substrate intermediate formed as the carbonyl double-bond is reformed.
2.Which statement describes a common feature of both the RNase A and Serine Protease mechanisms? a.A deprotonated serine acts as a nucleophile b. a covalent enzyme-substrate intermediate is formed c. Water is protonated by a Histidine to generate an acidic hydronium ion. d. a Histidine acts as a Bronsted base to remove a proton from an alcohol group.
Explanation / Answer
Question 1
Answer is C
the oxyanion hole describes the stabilization of the tetrahedral intermediate where H-bonding lowers the energy of the negatively charged oxygen resulting from a nucleophilic attack on the carbonyl carbon.
The Oxyanion is a catalytic component os serine protease.
he oxyanion Hole is by NHsof Gly193 and Ser 195 and these acts as the backbone. They are involved in the formation of pockets of positive charge and activate carbonyl of scissile peptide and produces stabilization of negatively charged oxyanion of the tetrahedral intermediate.
The oxyanion is structurally related catalytic triad.
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