Here is a scheme describing the keto-enol tautomerization reaction. Design the catalytic site of an enzyme...

Here is a scheme describing the keto-enol tautomerization reaction. Design the catalytic site of an enzyme that would accelerate the rate of this reaction. The rate enhancement should be as great as possible. Draw the amino acids that would be involved in the reaction and the electron flow during each reaction step. Remember that the enzyme has to be regenerated at the end of catalysis.

Expert Solution

In organic chemistry, keto–enol tautomerism refers to a chemical equilibrium between a keto form (a ketone or analdehyde) and an enol (an alcohol). The enol and keto forms are said to be tautomers of each other. The interconversion of the two forms involves the movement of an alpha hydrogen and the shifting of bonding electrons; hence, the isomerism qualifies as tautomerism.

Enzymes are macromolecules that help accelerate (catalyze) chemical reactions in biological systems. This is usually done by accelerating reactions by lowering the transition state or decreasing the activation energy.

Catalysis happens at the active site of the enzyme. It contains the residues that directly participate in the making and breaking of bonds. These residues are called the catalytic groups. Although enzymes differ widely in structure, specificity, and mode of catalysis a number of generalizations concerning their active sites can be made

queen_honey_blossom answered 7 months ago

What is an advantage of an enzyme with multiple domains each with a different catalytic site?

A zinc ion in the active site of an enzyme can speed up the reaction by:...

A zinc ion in the active site of an enzyme can speed up the reaction by: A. Making a bound water molecule a more powerful nucleophile by drawing electron density toward itself and facilitating deprotonation of the water B. Orienting substrates for reaction C. Stabilizing an anionic intermediate D. All of these E. None of these The role of serine at the active site of serine proteases is to act as a ___ catalyst, while the histidine residue serves as...

the kcat of an enzyme is 1875 sec ^-1, catalytic efficeny of same enzyme is 7.5*10^7,...

the kcat of an enzyme is 1875 sec ^-1, catalytic efficeny of same enzyme is 7.5*10^7, what is the km of enzyme?

The active site of an enzyme is a small portion of the enzyme molecule What is...

The active site of an enzyme is a small portion of the enzyme molecule What is the function of the rest of the huge molecule? Check all that apply. To pass through cell membranes. To provide sites for enzyme control and regulation. To hold the substrate in place. To stabilize the three-dimensional structure of the enzyme. To align the active-site functional groups that catalyze the reaction.

3a. The catalytic mechanism of an enzyme involves nucleophilic attack on the substrate by an active...

3a. The catalytic mechanism of an enzyme involves nucleophilic attack on the substrate by an active site cysteine. Normally, this cysteine has a pKa of 8.2. If the cytoplasm of the cell is pH 7.2 and the pH of the mitochondrial matrix is 8.2, predict whether this enzyme is a better catalyst in the cytoplasm or mitochondria. Explain

Ammonia is produced by the catalytic reaction of nitrogen and hydrogen. A) Write the chemical reaction...

Ammonia is produced by the catalytic reaction of nitrogen and hydrogen. A) Write the chemical reaction and balance it. Determine the stoichiometric coefficients. B) If 15 mol/sec of H2 is fed to the reactor, determine the amount of N2 required if a 20.% excess (of N2) is desired. C) If 5.0 mol/sec of H2 exits the catalytic reactor, determine: i) ξ. ii) the number of moles of all three components exiting the reactor. iii) the conversion of H2...

1. The active site of an enzyme usually consists of a pocket on the enzyme surface...

1. The active site of an enzyme usually consists of a pocket on the enzyme surface lined with the amino acid side chains necessary to bind the substrate and catalyze its chemical transformation. Carboxypeptidase, which sequentially removes the carboxyl-terminal amino acid residues from its peptide substrates, consists of a single chain of 307 amino acids. The two essential catalytic groups in the active site are furnished by Arg145 and Glu270 . a. How many amino acid residues apart are these...

define the following terms: biotechnology, plasmid, selectalbe marker, multiple cloning site, restriction enzyme, restriction enzyme site,...

define the following terms: biotechnology, plasmid, selectalbe marker, multiple cloning site, restriction enzyme, restriction enzyme site, DNA transformation, annealing

Which of the following binds to the active site of an enzyme?

Which of the following binds to the active site of an enzyme? water product substrate any other enzyme none of the above

Understand the following enzymatic terms: substrate, enzyme, active site, induced fit, enzyme specificity, product, enzyme /...

Understand the following enzymatic terms: substrate, enzyme, active site, induced fit, enzyme specificity, product, enzyme / substrate complex, cofactors and coenzymes

Question