Which of the following statements is correct for the reaction catalyzed by chymotrypsin?○ The substrate carbon atom bonded to Ser195 in the acyl enzyme intermediate has a tetrahedralgeometry○ The Ser195 hydroxyl oxygen atom is the catalytic nucleophile for the deacylation phase of the overallreaction mechanism○ The oxyanion hole accelerates the reaction by tightly binding the substrate carbonyl oxygen at thepeptide bond that is cleaved○ Asp102 stabilizes the tautomeric state of the catalytic histidine○ The first reaction product contains a proton derived from an active-site water molecule

For the reaction catalyzed by chymotrypsin, the correct statement is:The substrate carbon atom…

Answered: Which of the following statements is…

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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This a reaction going on in your muscle cells right this very minute:
You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new enzyme uses the same catalytic triad and the same reaction mechanism as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non- ionizable R groups.A) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn- Phe- Lys substrate ending your answer with the product and free enzyme.
An enzyme with an unknown reaction mechanism has been isolated and is being investigated in the lab. Based on the information given below, propose one or more specific catalytic strategies (covalent, acid-base, and/or metal ion catalysis) used by the enzyme and predict the role of each catalytic residue in the enzyme's reaction cycle. Explain your reasoning. (a) Mapping of the active site with substrate analog showed that it contains a critical Ser residue. (b) Studies conducted in buffers of varying pH showed that the enzyme is sensitive to pH changes and has two catalytically important residues with pKa values of ~10.5 and ~4.0. (c) Substitution of the Ser residue with Ala resulted in a five-fold increase in the KM but had no effect on the kcat. (d) The reaction rate was insensitive to the addition of metal chelators such as EDTA and EGTA.
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The degradation of CH3 (CH₂ )10 - COOH via the beta-oxidation pathway requires: 6FAD + 6NAD+ + 5C0A-SH + 6H₂O 5FAD + 5NAD+ + 6C0A-SH+ 5H₂O 5FAD + 5NAD + 5C0A-SH + 5H₂0 6FAD + 6NAD+ + 6C0A-SH + 6H₂O
Intermediates of a pathway are shown in the following scheme. Using curved arrows, show the mechanism of each step labeled with a blue letter. Draw out abbreviated structures of the coenzymes, so that you can effectively show all arrow pushing. You may abbreviate the coenzymes by putting R groups on the molecule, but do draw out the parts of the structure that are involved in the arrow pushing. Some of the transformations will require you to show multiple structures to show all of the arrow pushing (particularly some of the coenzyme-mediated steps). You do not need to show specific amino acid residues that perform the catalysis. You can abbreviate acidic amino acid residues “Enz–B–H” and basic residues “B–Enz”.
Many metabolites are maintained at steady‑state concentrations that are far from equilibrium. A comparison of ?′eq and ? , the mass‑action ratio, can determine whether a metabolic reaction is far from equilibrium. The equation for this equilibrium is, fructose 6-phosphate+ATP↽−−⇀fructose 1,6-bisphosphate+ADPCalculate ?′eq for this reaction at ?=25.0 ∘C . Δ?∘′=−14.2 kJ/mol ?′eq=
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