When lead acts as a poison, it can do so either by replacing another ion (such as zinc) in the activesite of an enzyme or by reacting with cysteine side chains to form covalent bonds.Which of these is irreversible and why?Match the items in the left column to the appropriate blanks in the sentences on the right.Reset Helpa covalent bondWhenoccurs between the active site (containing cystein) and the inhibitor (lead),replacement of an ionthe substrate is excluded or the catalytic reaction is blocked.an ionic bondWhenoccurs and the inhibitor (lead) replaces another ion.reaction with side chainsTheis an example of a permanent, irreversible change.ion exchangeTheis an example of a change that can be reversed.

Inhibition can be broadly divided into two types. Reversible Inhibition : Here the the inhibitor…

Answered: When lead acts as a poison, it can do…

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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The concept of determining which reactant is limiting and which is in excess is akin to determining the number of sandwiches that can be made from a set number of ingredients. Assuming that a cheese sandwich consists of 2 slices of bread and 3 slices of cheese, determine the number of whole cheese sandwiches that can be prepared from 36 slices of bread and 51 slices of cheese.
For the chemical reaction that results in the formation of a peptide bond between two amino acids, AG = +4 kcal/mol. Based on this information, which of the following labels would be appropriate to describe this reaction? O Exergonic O Hydrolysis O Redox O Endergonic
Some enzymes can be regulated by covalent modification, in which a group is covalently bonded to an amino acid side chain. Phosphorylation of side chains is a common regulatory covalent modification. In this essay, you will explore phosphorylation of side chains. Compare and contrast the types of interactions a free alcohol side chain such as serine could make with that of a phosphorylated alcohol such as phosphoserine (pSer). Could this modification affect the 3D structure of the protein? How? Imagine you are trying to separate a protein containing an unphosphorylated S residue from the same protein containing a pSer residue. Discuss how you could use ion-exchange chromatography to separate these two proteins
Amylase is an enzyme that breaks bonds between the monosaccharides in starch in order to detach these monosaccharides from the chain of starch. Based on this description, which type of reaction does amylase catalyze? A) Osmotic reactions B) Peptide reactions C) Dehydration reactions D) Hydrolysis reactions
Amylose is comprised of glucose monomers connected by what kind of glycosidic bond? a (1 -->4) a (1 --> 6) b (1 --> 4) b (1 --> 6) None of the above
The following reaction would most likely be catalyzed by an enzyme of which class? sucrose + H2O → glucose + fructose
Which of the following statements is false regarding an enzyme's ability to catalyse a reaction? an enzyme provides a reaction surface and a hydrophilic environment for the reaction to take place an enzyme binds reactants such that they are positioned correctly and can attain their transition-state configurations an enzyme allows the reaction to go through a more stable transition state than would normally be the case an enzyme can weaken bonds in reactants through the binding process
The above monosaccharides (glucose and galactose) are held together in the disaccharide lactose by: disulfide bonds ether bonds glycosidic bonds ester bonds peptide bonds
The above glucose monosaccharides are held together in the maltose sugar by: glycosidic bonds ether bonds disulfide bonds ester bonds peptide bonds
Use drawings to explain how an enzyme (such as hexokinase, mentioned in the text) can distinguish its normal substrate (here d-glucose) from the optical isomer l-glucose, which is not a substrate. (hint: remembering that a carbon atom forms four single bonds that are tetrahedrally arranged and that the optical isomers are mirror images of each other around such a bond, draw the substrate as a simple tetrahedron with four different corners and then draw its mirror image. using this drawing, indicate why only one optical isomer might bind to a schematic active site of an enzyme.)
which of the following describes an enzyme ALLOSTERIC site?
The breakdown of large molecules by the enzymatic addition of water is an example of a(n) _____ reaction?

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When lead acts as a poison, it can do so either by replacing another ion (such as zinc) in the active site of an enzyme or by reacting with cysteine side chains to form covalent bonds.