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

Solutions

Expert Solution

If an enzyme is having multiple domain, each with a different catalytic site, it means that the enzyme can bind to more than one types of substrate at one time.

This is particularly important during condensation or anabolic reaction. In these reactions, water, one or more than one types of monomers are used for the synthesis of polymers. So, at one time, the enzyme can bind to all the different types of monomers and water and thereby synthesizing polymers.

Apart from binding substrate molecules, this domain are also responsible for binding cofactors and activator proteins. These accessory molecules help in increasing the rate of catalytic reaction.

Sometime inhibitor and repressor molecules can also bind to this site thereby decreasing the rate of reaction.

Hence, the overall advantage of having multiple domain in enzyme is to bind more than one type of substrate at one time and also to bind activator in order to increase the rate of reaction.

Please give a good rating.

gladiator answered 1 year ago

Next > < Previous

Related Solutions

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.

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

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.

Which enzyme in each of the following pairs would be more limited in its catalytic scope?...

Which enzyme in each of the following pairs would be more limited in its catalytic scope? A) An enzyme that exhibits linkage specificity or an enzyme that exhibits absolute specificity? and B) An enzyme that exhibits group specificity or an enzyme that exhibits stereochemical specificity?

How does an enzyme lower the activation energy? What are the specific catalytic mechanisms? What are...

How does an enzyme lower the activation energy? What are the specific catalytic mechanisms? What are the three types of specific catalytic mechanisms?

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?

What are enzymes? What is the active site of an enzyme? What does the term substrate...

What are enzymes? What is the active site of an enzyme? What does the term substrate mean?

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

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...

Distinguish the different aspects or domains of change in the health industry and how those domains...

Distinguish the different aspects or domains of change in the health industry and how those domains impact leadership capability, and explain how the synergy of those changes impacts leadership capability and organizational success.

Subjects