8. Structures of three coenzymes involved in Phase II conjugation reactions areshown below. For each coenzyme, circle the portion of the coenzyme that istransferred during metabolic reaction.NH,CHNH,COOCH,H2COHCHНОO-UDPHCHHОНононUDP-GlucuronateS-Adenosylmethionine (S-AdoMet)SCoAcetylSCo

Coenzymes are organic nonprotein molecules that bind to the apoenzyme to form the active holoenzyme.…

Answered: 8. Structures of three coenzymes…

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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2. (Part A) Coenzyme-dependent enzymes can catalyze the general transformations shown below. What would be the best coenzymes to use for the two steps in the scheme, and why? R CO₂H A R SCOA B R R
1. - - Substrate Enzyme - 1 2 3 BOO - Look at the above diagram and understand what is being shown. Explain AND draw a graph depicting how the rate of the reaction depicted here is changing. ☐ L 2. How will the rate of the reaction change with time after 3? How can we increase the rate of the reaction after 3? I 100 B L
List the systematic classification of anzymes according to then Enzyme Commission indicating the class, subclass and sub-sub-class and give the description of each reaction
label all 5 identified regions in the active site, (labels like basic catalytic residue, acidic catalytic residue, catalytic nucleophile, etc.)
match the coenzyme on the left with the reaction in which they participate on the right
Draw the first step of lipid hydrolysis using water as a nucleophile
3
5
1. Depict the structure features in the active site of cysteine protease 2. provide a step-wise reaction mechanism to show the hydrolysis of the peptide bond catalyzed by a cysteine protease
9. Bacteria can synthesize tryptophan, tyrosine, and phenylalanine through a series of biochemical reactions. All three amino acids are derived from the same precursor molecule, as shown in the diagram below. OH но OH Common Precursor Anthranilate Chorismate Synthase Mutase OH NH2 00 Trp Precursor Tyr/Phe Precursor a. A majority of this precursor is used by the enzyme chorismate mutase to synthesize another precursor that is used to make phenylalanine or tyrosine. Experimental data shows that when there is a high concentration of phenylalanine in a cell, more tryptophan is produced. This data also suggests that phenylalanine binds to chorismate mutase but does not bind to the enzyme's active site. Use what we learned in class to describe how this binding could regulate chorismate mutase's activity and result in more tryptophan being produced. b. The common precursor is also a substrate for a second enzyme, anthranilate synthase. The product of that reaction is a precursor for…
What kind of catalysis is cysteine driving in this picture? S Los i fy R……—NHR N-H---S O. N-H H-N H-N. O Metal catalysis Covalent catalysis Base catalysis O Acid catalysis NHR²
1 Give the systematic names and the first three digits in the E.C. classifications of the enzymes catalysing the following reactions: (Note: it should be possible to deduce the classification and make a reasonable attempt at the systematic name from the information given in Chapter 1.) (a) R.CO.CH,CH,.Ñ(CH,); + H,0 = R.cO + HOCH,CH,.Ň(CH,)3 acyl choline acid anion choline (b) H,N.ÇOPO + H;N(CH,),.CH.Co, = H,N.C.NH(CH2)3.C CH.CO, +P, * NH3 * NH3 L-ornithine carbamoyl phosphate citrulline H (c) ATP + H,N.CHCO, + H,Ñ.CHCO, H,N.CH.CN.CHCO, + ADP + P, CH3 CH3 H,C Ö CH; D-alanine D-alanine D-alanyl-alanine ÇH,OH (d) Ç=0 + NADH + H* = ÇHOH + NAD ČH,OH glycerol ČH2OH dihydroxyacetone (e) СНОН 2 C=0 + CHOH СНОН CH,OH CH,OPO; ČHOH D-glyceraldehyde-3-phosphate CH,OPO? dihydroxyacetone-phosphate D-frucrose-1,6-bisphosphate (f) NADH + 2 ferricytochrome b, = NAD* +2 ferrocytochrome bs (g) UDP-galactose 2 UDP-glucose (glucose and galactose are aldohexoses differing in configuration at C4)

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