0
State the function of polar regions of amino acids on the active site of the enzyme?
Wiki User
∙ 9y ago
The function of polar regions of amino acids on the active site of the enzyme is that it allows the reaction to take place more easily. The active site is the place where the actual chemical reaction takes place.
Wiki User
∙ 9y ago
Add your answer:
Earn +20 pts
What happens when an enzyme is denatured?
When an enzyme is denatured the active site which allows it to catalyze reactions is destroyed, rendering the enzyme useless. This process is irreversible but the remains are recycled to form new enzymes.
Competitive inhibitors block the entry of substrate into the active site of an enzyme On what properties of an active site does this primarily depend?
The enzymes ability to stretch reactants and move them towards a transition state
Why are transition state analogs good inhibitors?
Enzymes are thought to function primarily by stabilizing the transition state of the reaction. By binding the transition state more tightly than either the substrates or the products, the enzyme lowers the energy barrier of the reaction. Thus a transition state analog will bind more tightly to the enzyme than either the substrates or the products, preventing them from binding to the enzyme and reacting.
The effect of substrate concentration on the rate of reaction of h202 and catalase?
As the substrate concentration increases, so will the enzyme activity and hence there will be a quick reaction. however, only up to a certain point ( where, if you drew a graph of the reaction, the line will level off ) as all the active sites in the enzyme are occupied and the reaction cannot go any faster. Here more enzymes will be needed to speed up the reaction.
How enzyme lowering the activation energy?
Enzymes lower activation energy by providing the substrates with an ideal environment for the certain reaction. Often, certain parts of the enzyme chain in the activation site will make the substrate more unstable by binding to it. This instability makes it easier to break down the substrate, or attach another molecule to it.
What happens when an enzyme is denatured?
When an enzyme is denatured the active site which allows it to catalyze reactions is destroyed, rendering the enzyme useless. This process is irreversible but the remains are recycled to form new enzymes.
What helps an enzyme to bind to a specific active site?
What? Enzyme doent look for another enzmes active site! it just look for its substrate to bind at in its active site! This will in turn make it to form any by products or convert it from the actual state!
Competitive inhibitors block the entry of substrate into the active site of an enzyme On what properties of an active site does this primarily depend?
The enzymes ability to stretch reactants and move them towards a transition state
What happens to enzymes when it performs its function?
An enzyme like other catalysts may change shape and/or enter an excited state temporarily while performing its function, but it returns immediately to the original shape and/or energy state upon completion thus consuming no energy in the process. However the reaction it catalyses may consume energy, but usually much less than would be needed without the assistance of the enzyme.
How many state regions does Kentucky have?
Kentucky has six state regions
When the enzyme is at its most active state an increase in the concentration of substrate will?
An enzymatic reaction is an equilibrium reaction and the determiners of rate include enzyme and substrate concentration. An increase in either enzyme or substrate concentration will increase the rate of the reaction until one or the other component becomes saturated, beyond its ability to react or be reacted at a higher rate.
What are the four mechanisms that get substrates to the transition state?
The four mechanisms that get substrates to the transition state are: Acid-base catalysis, where protons are transferred between the enzyme and substrate to stabilize the transition state. Covalent catalysis, where the enzyme forms a transient covalent bond with the substrate to lower the activation energy. Metal ion catalysis, where metal ions in the active site of the enzyme participate in the catalytic reaction. Catalysis by proximity and orientation, where the enzyme brings the substrates in close proximity and in the correct orientation to facilitate the reaction.
How is genetic engineering helpful to tay sachs disease?
. One potential treatment focuses on the lack of the hexosaminidase A enzyme. If the enzyme can be replaced, then the GM2 deposits could be broken down into their component parts, and nerve cells could return to a state of proper function.
Why are transition state analogs good inhibitors?
Enzymes are thought to function primarily by stabilizing the transition state of the reaction. By binding the transition state more tightly than either the substrates or the products, the enzyme lowers the energy barrier of the reaction. Thus a transition state analog will bind more tightly to the enzyme than either the substrates or the products, preventing them from binding to the enzyme and reacting.
How many regions are in the state of Alabama?
There are 5 regions
How many regions does state of California has?
4 regions
Is the enzyme that catalyzes glycogenolysis always present in active form?
I think you're referring to glycogen phosphorylase, which is an enzyme that catalyzes the reaction where glycogen is turned into a glucose-molecule, therefore making it available for transformation to energy. Glycogen phosphorylase comes in two forms, A and B. Usually, the A form is considered the active form, whilst B is the inactive form. That is a modified truth, since both of these forms can exist in a T (tense) inactive state and R (relaxed) active state, depending on the presence of ADP (residue after phosphorylation of ATP). But usually, A is in its R state and B is in its T state. So for the sake of argument, we say A is active and B is inactive. So the short answer would be 'No'. For example, hormones such as epinephrine, insulin, and glucagon regulate glycogen phosphorylase. Essentially, epinephrine and glucagon promotes the A form (by activating phosphorylase kinase, an enzyme that transforms A into B), and insulin promotes the B form (by inhibiting the phosphorylase kinase).
