c) In the chanism of alcohol dehydrogenase reducing acetaldehyde to ethanol, NADHdonates a hydride to the carbonyl C, and the oxyanion is transiently stabilized by the Zn2+divalent cation (see figure on first page), which is then protonated to form the final product.If one assumes that 4-iodopyrazole was bound similarly to the substrate, then which atomsof the inhibitor would be equivalent to the atoms of acetaldehyde? Mark the figure belowwith the atom of 4-iodopyrazole equivalent to each of the 3 heavy atoms in acetaldehyde.(Use the atom identifiers to identify each one unambiguously: N1, N2, C3, C4, C5, 14.)carbonyl CHCcarbonyl OCH3methyl CBased on this, do you see any residue likely to serve as a proton donor to the oxygenof the ethanol alkoxide intermediate (CH3-CH2-O') in the last step of themechanism?If so, which residue is it?Choose the correct ending for each statement, as best you can:The binding site for NAD*/NADH isshared between 2 domains of ADH.almost exclusive in one domain of ADH. shared between 2 domains of ADH.almost exclusive in one domain of ADH.The active site of ADH (where the chemistry takes place) isshared between 2 domains of ADH.almost exclusive in one domain of ADH.

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Answered: c) ogenase reducing acetaldehyde to…

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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Draw the major product of the following Sonogashira coupling reaction. [Pd], pyrrolidine, TBAB + =Ph H₂O, reflux Draw the major product(s) of the following alkene (olefin) metathesis reaction. Ar + N ROW RO
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 tetrahedral geometry ○ The Ser195 hydroxyl oxygen atom is the catalytic nucleophile for the deacylation phase of the overall reaction mechanism ○ The oxyanion hole accelerates the reaction by tightly binding the substrate carbonyl oxygen at the peptide 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
1) Sketch out the schematic diagram for the enzymatic mechanism of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) Please provide the structure of the functional groups of the substrate and enzyme involved in the reaction at each step (rest of the structure can be indicated as R) Indicate clearly the flow of the electrons at each step Indicate in short form the cofactor involved and the acid or basic groups of the enzyme involved
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What are the amino acids of the catalytic triad of chymotrypsin? State the mode of catalysis shown by each of the amino acids that you have named. (a) (b) Predict what will happen if aspartic acid of the triad is replaced by asparagine. (c) Briefly explain the role of the oxyanion hole for the catalysis of chymotrypsin.
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make a schematic diagram of BChE/AChE inhibitory determination Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide(AChI) molecules were utilized as substrate compounds of the reaction. Inthis regard, 5,5′‐dithio‐bis(2‐nitro‐benzoic acid) compound (DTNB) wasused to estimate BChE/AChE activity. In summary, 100 μL Tris buffersolution (HCl, 1.0M, pH 8.0, Tris) and variety of concentrations of thesample solution (50‐200 mL) were added in deionized water and also20 μL of BChE/AChE enzymes solutions added. The mixture was thenincubated for 10 minutes at 20°C. Finally, 50 μL of DTNB (0.5 mM and25 mL) BChI/AChI were added to the incubator mixture. The reactionwas also started by adding 50 μL BChI/AChI. The activity of theseenzymes was evaluated using spectrophotometric spectra with awavelength of 412 nm.
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In the Enzyme Commission database system, an enzyme with the designation 4.3.2.1 would catalyze which reaction below? Select one: O a. The conversion of an alcohol to an aldehyde O b. The conversion of an alcohol to a phosphate O c. The conversion of an alcohol to an ether o d. The conversion of an alcohol to an alkene A buffer molecule is protonated at pH 9. Adding this buffer to a reaction greatly increases the rate of reaction at pH 9.0. What is true about the reaction? Select one: O a. The buffer is a specific base Ob. It is catalyzed by acid OC. It is catalyzed by base o d. The buffer is a specific acid
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