Esterase hydrolyzes ester bonds. For simplicity, only the amino acids whose side-chainsinteract with the substrate are shown. Each circled interaction is important for the bindingof the substrate to the enzyme.substratex CH,-OCH ZH3CCH, H,CCH,Esteraseactive siteFull activity of esterase is observed at 37°C and a pH of 7.4. You isolate the active form ofesterase, subject it to a high salt (high sodium chloride) concentration and show that it cannot bindthe substrate. You then return the sample to the original conditions and measure the substratebinding ability of the esterase again.Would the esterase bind to its substrate when returned to the pretreatment conditions(Yes/No)? Explain.

Ans. Yes. Yes, the esterase will most likely bind to the substrate when returned to the…

Esterase hydrolyzes ester bonds. For simplicity, only the amino acids whose side-chains interact with the substrate are shown. Each circled interaction is important for the binding of the substrate to the enzyme. substrate x LCH- CH, CH Z CH, H,C CH, H3C. Esterase active site

Esterase hydrolyzes ester bonds. For simplicity, only the amino acids whose side-chains interact with the substrate are shown. Each circled interaction is important for the binding of the substrate to the enzyme. substrate x LCH- CH, CH Z CH, H,C CH, H3C. Esterase active site

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

What type of enzyme is needed to catalyze the following reaction?
What is X in the following biochemical pathway? O O O O O NH3 + A. A ош O R CH a-ketoglutarate coenzyme PLP aminotransferase CH3 D. glutamate 0 B. || NH R. X 0™ coenzyme TPP decarboxylase E. 0™ C. CH CO₂ OH O™ R. H 'Н
According to the following graph, the activity of the enzyme decreases more sharply at high temperature than at low temperature. What are the reasons for this observation? Enzyme activity Optimum temperature Temperature, °C I. As temperature is increased, the substrate binding slowly becomes poorer. II. As temperature is decreased, the enzyme moves more slowly and so reacts more slowly. III. At higher temperatures, the enzyme is denatured and stops working entirely. IV. Temperature has no effect on enzyme activity. ○ I only O IV only I and III O II and III
How does changing the concentration of enzyme at a fixed concentration of substrate affect the rate of decomposition of H2O2?
explain each graph above about enzymes and the factors affecting enzymatic activity.
Questions #58 and #59 please
Examine this depiction of the initial steps of catalysis for a proteolytic enzyme. Oxyanion hole 93 with In 1-2 sentences, describe the role being played by the amino acid hydroxyl side chain in the step labeled 2. In 1-2 sentences, describe the role of the oxyanion hole. In 1-2 sentences, describe the role of the His is the step labeled 3.
Triosephosphate isomerase (TIM) catalyzes the conversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate. The enzyme’s catalytic groups are Glu 165 and His 95. In the first step of the reaction, these catalytic groups function as a general-base and a general-acid catalyst, respectively. Propose a mechanism for the reaction.
What is the expected result if the enzyme monoamine oxidase is treated with the substrate analog named N,N-dimethylpropargylamine? H3C `N I CH3 N,N-dimethylpropargyl amine The product propargyl aldehyde (H-C=C-CH=O) will be formed and released. The product propargyl alcohol (H-CEC-CH₂-OH will be formed and released. The enzyme will be rapidly and covalently (irreversibly) inhibited. The enzyme will be reversibly and competitively inhibited in the presence of this substrate analog. a. b. monoamine oxidase C. d. MAO + O₂
1) A new enzyme was isolated from underneath Antarctica! It catalyzes the following reaction! Zn+2 OH CI HCI Based on what you know, what is the role of the Zn+2 in this enzyme reaction? To answer this, show what Zn+2
The following graph of an enzyme catalyzed reaction what does B represen Rate of reaction A B maximum velocity minimum velocity competitive inhibition non-competitive inhibition
Derive a general equation for the relative activity (a) of an enzyme in the presence of a competitive inhibitor.