The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and pther acyl esters. Name the amino acid residue, the side chain of the residue, and the type of bond/linkage involved in the formation of the acyl-emzyme complex during catalysi

The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and pther acyl esters. Name the amino acid residue, the side chain of the residue, and the type of bond/linkage involved in the formation of the acyl-emzyme complex during catalysi

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 21P: Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved...

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Metabolic pathways

Metabolism is defined as the group of life-supporting, enzyme-mediated chemical reactions in organisms. A metabolic pathway is a set of these chemical reactions that involve anabolism (synthesis of complex biomolecules) and catabolism (breakdown of biomolecules into small molecules) that occur inside a cell. Metabolites are the reacting substances, products, and intermediate substances of an enzymatic process that are altered by a series of chemical events catalyzed by enzymes.

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The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and other acyl esters. Name the amino acid residue, the side chain of the residuee and the type of bonding/linkage involved in the formation of the acyl-enzyme complex during catalysis.
The active site of an enzyme has the following amino acid residues as critical mediators of catalysis: Ser-134, His-347, Tyr-121 and Glu - 406. What are the most likely specific mechanisms of catalysis by these amino acid residues?
the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.
Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.
can somone please List the components of the enzyme complex involved in the transition step and Simply describe what does each component does? 1. 2. 3. ect..
Enolase has a glutamic acid residue in its active site. Describe the experiment that was done that provided evidence for the proposed function of the glutamic acid residue in catalysis by enolase.
UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?
In enzyme catalysed reactions, the energy level of the enzyme/substrate (or ES) complex is higher (or raised) compared to the uncatalyzed reaction. List 4 factors that contribute to this raised energy level and explain how each of these factors contribute to the higher energy level of the ES complex
The amino acid histidine has been found to participate in both acid and base catalysis in many enzymatic reactions. Which of the following describes histidine? A. Its R group acts as proton donor at pH 7.0 B. Its R group acts as electron pair acceptor at pH 7.0 C. Its R group acts as proton acceptor at pH 7.0 D. Its R group helps in the proteolytic activity by acting as both proton donor and proton acceptor at pH 7.0
Briefly describe the induced-fit conformational change when hexokinase binds its substrate.
In what type of catalysis does Lys345 engage during the very first step of enolase's reaction cycle? Explain, in your own words, specifically why and how Lys345 falls into the category you chose.
Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?