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.

Hi! Since we are authorized to answer only one question at a time, i am answering the first…

Answered: c) ogenase reducing acetaldehyde to…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter17: Metabolism: An Overview

Section: Chapter Questions

Problem 14P

See similar textbooks

Similar questions

Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for the methylmalonyl-CoA mutase (see problem 14), write reasonable mechanisms for the following reactions shown.
If you were to determine the P/O ratio for oxidation of a-ketoglutarate, you would probably include some malonate in your reaction system. Why? Under these conditions, what P/O ratio would you expect to observe?
Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.
Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. _____________________1. Name: alkaline phosphataseReaction: a phosphate monoester + H2O = an alcohol + phosphate_____________________2. Reaction: L-threonine = D-threonine.Other information: Inverts both chiral centers, a racemase. _____________________3. Name: glycine-N-acylaseReaction: acyl-COA + glycine = CoA + N-acylglycine_____________________ 4. Name: lysine decarboxylaseReaction: L-lysine = cadaverine + CO2 _____________________5. Name: methanol dehydrogenaseReaction: methanol + NAD+ = formaldehyde + NADH + H+ _____________________6. Name: citryl-CoA synthetaseReaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA_____________________7. Name: D-xylulose reductaseReaction: xylitol + NAD+ = D-xylulose + NADH + H+ _____________________8. Name: cellobiose phosphorylaseReaction: cellobiose phosphate =…
In Bacillus subtilis, threonine is metabolized by the following sequence of reactions: (a) oxidation; (b) decarboxylation;(c) transamination; and (d) oxidation to produce pyruvate. Outline this sequence of steps, show the structures of thesubstances, use abbreviations for the cofactors, and show any enzyme-bound coenzymes. What type of enzyme bound intermediate is likely for reaction (d)?
If you were to determine the P/O ratio for oxidation of α-ketoglutarate,you would probably include some malonate in your reaction system. Why?Under these conditions, what P/O ratio would you expect to observe?
If a 0.1 M solution of glucose 1- phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Calculate Keq and ΔG′° for this reaction.
In many biochemical reactions which involves the formation of an enolate intermediate, the carbonyl oxygen of the substrate is coordinated to a divalent metal ion (usually zinc or magnesium) in the active site. Explain with structural drawings, how this ion-dipole interactions affect the acidity of the a-protons?
Write a balanced equation for each of the following reactions or reaction sequences. (a) The reaction catalyzed by PFK-2 (b) The conversion of 2 moles of oxaloacetate to glucose (c) The conversion of glucose to UDP-Glc (d) The conversion of 2 moles of glycerol toglucose (e) The conversion of 2 moles of malate to glucose-6-phosphate
In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.
The metabolism of alcohol pathway is showed in the figure characterized by biotransformation of: (Figure : Ethanol Metabolism Pathway - ADH : Alcohol dehydrogenases, ALDH: Aldehyde dehydrogenase ) (a) reaction phase I with two oxidations (b) reaction phase II with oxidation and sulfonation (c) reaction phase II with two hydrolysations (d) reaction phase II with two oxidations (e) reaction phase I with hydrolysis and oxidation

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS