Homework Help is Here – Start Your Trial Now!
Science
Biochemistry
c) ogenase reducing acetaldehyde to ethanol, NADH donates 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 atoms of the inhibitor would be equivalent to the atoms of acetaldehyde? Mark the figure below with 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 C HC carbonyl O CH3 methyl C

c) ogenase reducing acetaldehyde to ethanol, NADH donates 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 atoms of the inhibitor would be equivalent to the atoms of acetaldehyde? Mark the figure below with 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 C HC carbonyl O CH3 methyl C

Biochemistry
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
See similar textbooks
icon
Related questions
Question
100%
c) In the chanism of alcohol dehydrogenase reducing acetaldehyde to ethanol, NADH donates 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 atoms of the inhibitor would be equivalent to the atoms of acetaldehyde? Mark the figure below with 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 C HC carbonyl O CH3 methyl C Based on this, do you see any residue likely to serve as a proton donor to the oxygen of the ethanol alkoxide intermediate (CH3-CH2-O') in the last step of the mechanism? If so, which residue is it? Choose the correct ending for each statement, as best you can: The binding site for NAD*/NADH is shared between 2 domains of ADH. almost exclusive in one domain of ADH.
Transcribed Image Text:c) In the chanism of alcohol dehydrogenase reducing acetaldehyde to ethanol, NADH donates 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 atoms of the inhibitor would be equivalent to the atoms of acetaldehyde? Mark the figure below with 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 C HC carbonyl O CH3 methyl C Based on this, do you see any residue likely to serve as a proton donor to the oxygen of the ethanol alkoxide intermediate (CH3-CH2-O') in the last step of the mechanism? If so, which residue is it? Choose the correct ending for each statement, as best you can: The binding site for NAD*/NADH is shared 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) is shared between 2 domains of ADH. almost exclusive in one domain of ADH.
Transcribed Image Text:shared between 2 domains of ADH. almost exclusive in one domain of ADH. The active site of ADH (where the chemistry takes place) is shared between 2 domains of ADH. almost exclusive in one domain of ADH.
Expert Solution
trending now

Trending now

This is a popular solution!

steps

Step by step

Solved in 2 steps with 2 images

SEE SOLUTIONCheck out a sample Q&A here
Blurred answer
Similar questions
Recommended textbooks for you
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON
SEE MORE TEXTBOOKS