Shown below is a substrate for a Elastase.CH,HNNHNH,Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw thecatalytic triad, and show the role of the oxyanion hole. Draw the complete structure of everyintermediate and product and PUSH ARROWS!

Elastase is a serine protease that cleaves a peptide bond at the C-terminal of amino acids, val,…

Answered: Shown below is a substrate for a…

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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1967, Rabin demonstrated that a single substrate reaction catalised by an enzyme that has a single binding site for the substrate, can show sigmoidal kinetics. Discuss this scenario so that it is clear why a plot of Vo versus [SJ at fixed total enzyme concentration will be sigmoidal.
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
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Predict the effect of each of the following amino acid substitutions on the KM and kcat of the enzyme-catalyzed reactions
5. Shown below are the first steps in the mechanism of a cysteine protease, which catalyses amide bond hydrolysis in a similar manner as serine proteases. (a) Complete this mechanisms, and (b) sketch the approximate reaction coordinate diagram for this catalyzed reaction relative to the uncatalyzed proteolysis. HN N HN cysteine protease
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There is total of 25 Enzymes and 27 Products that should be shown on this pathway
protease mechanism: you isolate a new protease which cleaves the peptide bond 2 aa residues before a F residue. You might expect to fınd... O An I residue in the S2'pocket AL residue in the S2 pocket O aV residue in the oxyanion hole An Lresidue in the catalytic triad in Michaelis-Menton kinetics, cutting the enzyme concentration in half will O will double the reaction rate O will not change Vo and Vmax will change Vo but not turnover number decrease Km by half
PLP can catalyze both \alpha, \beta elimination reactions and \beta, \gamma - elimination reactions. Propose a mechanism for the following PLP - catalyzed \beta, \gamma elimination
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)
38. The shown reaction is one of the four repeating steps during fatty acid biosynthesis. Which of the following statements is correct? 유 CH3-C-CH₂-C-S-ACP A B OH 유 CH3-C-CH₂-C-5-ACP → A. The small molecule in box A is NADPH + H* B. It is the second reduction reaction during fatty acid biosynthesis C. Both A and B D. Neither A nor B

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Shown below is a substrate for a Elastase. -CH, NH NH. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!! O