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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During glycogen synthesis, glucose-1P is converted into a molecule called UDPG. This reaction also cleaves uridine triphosphate (UTP) forming uridine monophosphate and pyrophosphate (PPi). Provide four reasons why UTP can be used to power this reaction (no diagrams necessary).
Which cytochrome P450-catalyzed reaction is shown below? R-CH2NH2 [R-CH=NH] Oxidation of aromatic amines Oxidative deamination Oxidative O-dealkylation Oxidative N-dealkylation para-hydroxylation R-CHO + NH3
Which of the following statements about ribozyme catalytic residues is INCORRECT? General acid catalysis requires the standarde nucleotide exchangeable proton acidities (represented by pKa values). Ribozymes work by lowering the AG‡ through transition state stabilization without changing the overall AG of the reaction. Some ribozymes cleave phosphodiester bonds, and like proteases, can be autocatalytic. There are fewer known classes of mammalian ribozymes than mammalian enzyles.
This a reaction going on in your muscle cells right this very minute:
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.
Which of the following statements regarding the catalytic mechanism of superoxide dismutase is true? The D residue does not participate in acid-base catalysis during the course of the catalyzed reaction All of the answers are true The coordinated Zn2+ participates in stabilizing Cu²+ in the reduction-oxidation reactions to consume O₂ The Cu²+ coenzyme is coordinated by H residues, positioning it precisely for consumption of 0₂ The overall reaction consumes two equivalents of O₂ and two proton equivalents in order to produces one equivalent H₂O2
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”.
Order the cofactors based on their use in the mechanism of the a-etogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 2 3 4 answer choices: lipoamide, biotin, 2 Fe - 2S cluster, TPP, NAD+, FAD
The following diagram shows reaction curves for aspartate transcarbamoylase (ATCase) with carbamoylphosphate and different concentrations of aspartate, in the absence of ATP (curve 1) and presence of ATP (curve 2). What do the shapes of the curves tell us about the ATCase enzyme? 2 جر [aspartate] It binds substrate through a sequential mechanism. It binds substte cooperatively. It obeys Michaelis-Menten kinetics. It binds substrate through a concerted mechanism.
Predict the effect of each of the following amino acid substitutions on the KM and kcat of the enzyme-catalyzed reactions
Match the following catalytic strategies with their example. Place a Letter on the picture. There are only two examples given. CH2OH CH2OH CH2OH CH2OH он он OH OH + H20 OH OH OH но H. но но OH OH OH OH OH OH A. Oxidoreducatase B. Transferase C. Hydrolase D. Lyase NH3 E. Isomerase F. Ligase R-CH-COO "ooc-CH2-CH2-C-COO Amino acid a-Ketoglutarate

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