Asp 102 His 57 -H-N [His] [His+] pH = pK₂ + log (AA [HA] = Ser 195 `N----H-O Identify the ways that His 57 enhances the nucleophilic power of Ser 195. Chymotrypsin is a digestive enzyme with a catalytic optimum between pH 7.8 and 8.0. However, due to the presence of gastri juice, chymotrypsin often functions in an environment of pH 5.5-7.0. The imidazole group of free histidine has a pK₂ of 6.0. Use the Henderson-Hasselbalch equation to determine the ratio of deprotonated to protonated His 57 imidazole moieties at pH 6.1. proton acceptor acid catalyst proton donor base catalyst O Aside from positioning, what do you think is the role of the Asp 102 residue? ○ It allows nucleophilic attack by His 57. [His] ratio. [Hist] It raises the pK₂ of His 57. It protonates His 57 prior to substrate binding. It decreases the
Asp 102 His 57 -H-N [His] [His+] pH = pK₂ + log (AA [HA] = Ser 195 `N----H-O Identify the ways that His 57 enhances the nucleophilic power of Ser 195. Chymotrypsin is a digestive enzyme with a catalytic optimum between pH 7.8 and 8.0. However, due to the presence of gastri juice, chymotrypsin often functions in an environment of pH 5.5-7.0. The imidazole group of free histidine has a pK₂ of 6.0. Use the Henderson-Hasselbalch equation to determine the ratio of deprotonated to protonated His 57 imidazole moieties at pH 6.1. proton acceptor acid catalyst proton donor base catalyst O Aside from positioning, what do you think is the role of the Asp 102 residue? ○ It allows nucleophilic attack by His 57. [His] ratio. [Hist] It raises the pK₂ of His 57. It protonates His 57 prior to substrate binding. It decreases the
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Proteases are enzymes that cleave peptide bonds using general acid–base catalysis. General acid–base catalysis relies on a proton donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues.
In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin’s active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding.
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