Enzymes notes 2 enzyme substrate complexes and factors affecting enzymes
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Enzymes Notes #2- Enzyme Substrate Complexes and Factors Affecting Enzymes. Agenda. Sign up for rewrite if you want to take it (today is last day) Video Notes Short Video Group Activity Planning and presentation Practice. Video. https://www.youtube.com/watch?v=XTUm-75-PL4. Enzymes.

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Enzymes notes 2 enzyme substrate complexes and factors affecting enzymes

EnzymesNotes #2- Enzyme Substrate Complexes and Factors Affecting Enzymes


Agenda
Agenda

  • Sign up for rewrite if you want to take it (today is last day)

  • Video

  • Notes

  • Short Video

  • Group Activity

    • Planning and presentation

  • Practice


Video
Video

  • https://www.youtube.com/watch?v=XTUm-75-PL4


Enzymes
Enzymes

  • Catalysts are substances that speed up chemical reactions.  Organic catalysts (contain carbon) are called enzymes.

  • Enzymes are specific for one particular reaction or group of related reactions.

  • Many reactions cannot occur without the correct enzyme present.

  • They are often named by adding “ASE" to the name of the substrate. Example: Dehydrogenases are enzymes that remove hydrogen.


Enzyme substrate complexes
Enzyme-Substrate Complexes

  • When a substrate binds to the active site of an enzyme it is said form a complex.

  • The original theory on how this worked was called the LOCK and KEY model

    • This was because the substrate shape fits into a specific enzyme because of it’s shape like a specific key fits only a specific lock


Lock and key model
Lock and Key Model

  • As the substrates bind to the enzyme active site they are brought closer together allowing the reaction to occur

  • Sometimes the active site changes shape to bring the substrates even closer together

  • The reaction occurs and the product(s) are released. The enzyme returns to it’s normal tertiary configuration


Induced fit theory most current
Induced Fit Theory – Most current

  • “Induced-Fit model” is very similar but it claims that the enzyme has the ability to slightly alter its shape. The two models basically work the same way.

  • The substrate molecule does not fit exactly in the active site. This induces a change in the enzymes conformation (shape) to make a closer fit.

  • After the reaction, the products are released and the enzyme returns to its normal shape.

  • Only a small amount of enzyme is needed because they can be used repeatedly.


Video1
Video

  • https://www.youtube.com/watch?v=V4OPO6JQLOE


Roles of enzymes
Roles of Enzymes

  • Some enzymes simply complex with substrates bringing them close together to react

  • Other enzymes participate in the reaction occuring:

    • Example: Trypsin

      • Trypsin digests protein by breaking peptide bonds

      • Active site contains 3 amino acids with R groups that interact with the peptide bonds

      • Breaks the bond and brings in water


Rate of reaction
Rate of Reaction

  • Reactions with enzymes are up to 10 billion times faster than those without enzymes.

  • Enzymes typically react with between 1 and 10,000 molecules per second. Fast enzymes catalyze up to 500,000 molecules per second.

  • Substrate concentration, enzyme concentration, Temperature, and pH  affect the rate of enzyme reactions.


Group activity
Group Activity

  • 6 groups:

    • Substrate concentration

    • Temperature

    • pH

    • Enzyme concentration

    • Competitive inhibitor

    • -non-competitive inhibitor (and heavy metals)

    • Use page 108/109 and handout to prepare presentation

      • What is it?

      • Why/How does it impact speed of reaction

      • Key characteristics

      • Use a diagram…


Substrate concentration
Substrate Concentration

  • At lower concentrations, the active sites on most of the enzyme molecules are not filled because there is not much substrate.  Higher concentrations cause more collisions between the molecules.  With more molecules and collisions, enzymes are more likely to encounter molecules of reactant.

  • The maximum velocity of a reaction is reached when the active sites are almost continuously filled. Increased substrate concentration after this point will not increase the rate.  Reaction rate therefore increases as substrate concentration is increased but it levels off.

Enzyme Active Site is Saturated

Rate of Reaction

Substrate Concentration


Enzyme concentration
Enzyme Concentration

  • If there is insufficient enzyme present, the reaction will not proceed as fast as it otherwise would because there is not enough enzyme for all of the reactant molecules.

  • As the amount of enzyme is increased, the rate of reaction increases. If there are more enzyme molecules than are needed, adding additional enzyme will not increase the rate. Reaction rate therefore increases as enzyme concentration increases but then it levels off.

Even when adding more enzymes, there isn’t any more available substrate to create product at a faster rate

Rate of Reaction

Enzyme Concentration


Effect of temperature on enzyme activity
Effect of Temperature on Enzyme Activity

Rate of Reaction

30 40 50

Temperature


Effect of temperature on enzyme activity1

Increasing the temperature causes more collisions between substrate and enzyme molecules. The rate of reaction therefore increases as temperature increases.

Effect of Temperature on Enzyme Activity

Rate of Reaction

30 40 50

Temperature


Effect of temperature on enzyme activity2

Enzymes denature when the temperature gets too high. The rate of reaction decreases as the enzyme becomes nonfunctional.

Effect of Temperature on Enzyme Activity

Rate of Reaction

30 40 50

Temperature


Temperature
Temperature rate of reaction decreases as the enzyme becomes nonfunctional.

  • Higher temperature causes more collisions between the atoms, ions, molecules, etc. It therefore increases the rate of a reaction – “Turnover Rate”. More collisions increase the likelihood that substrate will collide with the active site of the enzyme.

  • Above a certain temperature, activity begins to decline because the enzyme begins to denature (unfold).

  • The rate of chemical reactions therefore increases with temperature but then decreases.

Rate of Reaction

30 40 50

Temperature


Denaturation
Denaturation rate of reaction decreases as the enzyme becomes nonfunctional.

  • If the hydrogen bonds within an enzyme are broken, the enzyme may unfold or take on a different shape. The enzyme is denatured.

  • A denatured enzyme will not function properly because the shape of the active site has changed.

  • If the denaturation is not severe, the enzyme may regain its original shape and become functional.

  • The following will cause denaturation:

    • Heat

    • Changes in pH

    • Heavy-metal ions (lead, arsenic, mercury)

    • Alcohol

    • UV radiation


Effect of ph on enzyme activity
Effect of pH on Enzyme Activity rate of reaction decreases as the enzyme becomes nonfunctional.

Each enzyme has its own optimum pH.

Pepsin Trypsin

Rate of Reaction

2 3 4 5 6 7 8 9

pH


pH rate of reaction decreases as the enzyme becomes nonfunctional.

  • Each enzyme has an optimal pH. Pepsin, an enzyme found in the stomach, functions best at a low pH. Trypsin, found in the intestine, functions best at a neutral pH.

  • A change in pH can alter the ionization of the R groups of the amino acids. When the charges on the amino acids change, hydrogen bonding within the protein molecule change and the molecule changes shape. The new shape may not be effective.

  • The diagram shows that pepsin functions best in an acid environment. This makes sense because pepsin is an enzyme that is normally found in the stomach where the pH is low due to the presence of hydrochloric acid. Trypsin is found in the duodenum (small intestine), and therefore, its optimum pH is in the neutral range to match the pH of the duodenum.

Pepsin Trypsin

Rate of Reaction

2 3 4 5 6 7 8 9

pH


Regulation of enzymes
Regulation of Enzymes rate of reaction decreases as the enzyme becomes nonfunctional.

  • The next several slides illustrate how cells regulate enzymes. For example, it may be necessary to decrease the activity of certain enzymes if the cell no longer needs the product produced by the enzymes.


Regulation of enzymes1
Regulation of Enzymes rate of reaction decreases as the enzyme becomes nonfunctional.

Cell can turn on DNA genes to build more enzymes when needed

genetic

regulation

regulation of enzymes

already produced

Cells can use certain chemicals to slow down existing enzymes

competitive

inhibition

noncompetitive

Inhibition

(next slide)


Competitive inhibition

In competitive inhibition, a similar-shaped molecule competes with the substrate for active sites.

Competitive Inhibition


Competitive inhibition1
Competitive Inhibition competes with the substrate for active sites.

This substrate cannot get into active site at this time

Active site is being occupied by competitive inhibitor


Noncompetitive inhibition
Noncompetitive Inhibition competes with the substrate for active sites.

Active site

Inhibitor

Altered active site

  • Another form of inhibition involves an inhibitor that binds to an allosteric siteof an enzyme.  An allosteric site is a different location than the active site.

  • The binding of an inhibitor to the allosteric site alters the shape of the enzyme, resulting in a distorted active site that does not function properly.

Enzyme


Noncompetitive inhibition1
Noncompetitive Inhibition competes with the substrate for active sites.

  • The binding of an inhibitor to an allosteric site is usually temporary.   Poisons are inhibitors that bind irreversibly. For example, penicillin inhibits an enzyme needed by bacteria to build the cell wall. Bacteria growing (reproducing) without producing cell walls eventually rupture.


Agenda1
Agenda competes with the substrate for active sites.

  • Homework Check

  • Assignment Answer Review

  • Quiz

  • Video

  • Notes

  • Demo Activity

  • Review Worksheet


Video2
Video competes with the substrate for active sites.


Feedback inhibition

The goal of this hypothetical metabolic pathway is to produce chemical D from A.

B and C are intermediates.

The next several slides will show how feedback inhibition regulates the amount of D produced.

Feedback Inhibition

A B C D

enzyme 1

enzyme 2

enzyme 3

Enzyme regulation by negative feedback inhibition is similar to the thermostat example. As an enzyme's product accumulates, it turns off the enzyme just as heat causes a thermostat to turn off the production of heat.


Feedback inhibition1

C and D will decrease because B is needed to produce C and C is needed to produce D.

The amount of B in the cell will decrease if enzyme 1 is inhibited.

X

X

X

Feedback Inhibition

A B C D

X

enzyme 1

enzyme 2

enzyme 3

Enzyme 1 is structured in a way that causes it to interact with D. When the amount of D increases, the enzyme stops functioning.


Feedback inhibition2

B, C, and D can now be synthesized. is needed to produce D.

B

When the amount of D drops, enzyme 1 will no longer be inhibited by it.

Feedback Inhibition

A B C D

X

X

X

C

D

enzyme 1

enzyme 2

enzyme 3


Feedback inhibition3
Feedback Inhibition is needed to produce D.

A B C D

X

enzyme 1

enzyme 2

enzyme 3

As D begins to increase, it inhibits enzyme 1 again and the cycle repeats itself.


Thyroxin and it s role in metabolic rate
Thyroxin and It’s Role in Metabolic Rate is needed to produce D.

  • Thyroxin: (AKA “Thyroid Hormone” “Thyroxine”)

  • - Thyroxin is a protein hormone that is secreted into the blood stream by cells of the thyroid gland

  • - The thyroid gland, which is located in the neck, accumulates iodine in order to produce the thyroxin hormone.

  • Thyroid Hormone Structure



- Thyroxin does not have a target organ; but instead, stimulates most of the cells of the body to metabolize at a faster rate. It does this by increasing the production of respiratory enzymes, as well as stimulating the increase of oxygen uptake.


- Thyroxin not only governs metabolic rate but it also helps regulate the growth and development of an individual.

- Thyroglobulin is the storage (precursor) form of Thyroxin. Iodine is required for thyroglobulin to be made. Without the presence of iodine the thyroid gland will increase in size in an effort to produce more Thyroxin.

- Unfortunately, a lack of Iodine in the diet, results in a lack of thyroxin in the body (HYPOTHYROIDISM). This often leads to a condition known as simple goiter.


Simple gloiter
Simple regulate the growth and development of an individual.Gloiter

- A simple goiter occurs when the thyroid gland is unable to produce a sufficient amount of Thyroxin, the thyroid cannot meet the metabolic demands of the body.

-The thyroid gland compensates by enlarging, this mechanism will often overcome a mild deficiency of the thyroid hormone.


Exophthalmic goiter graves disease
Exophthalmic Goiter (Graves’ disease) regulate the growth and development of an individual.

This type of Goiter is not caused by a lack of thyroxin but rather by the excessive production of the thyroid hormone (HYPERTHYROIDISM). –

- This condition is characterized by an enlarged thyroid gland, protrusion of the eyeballs, tachycardia (super fast heart rate) and nervous excitability.


Hypothyroidism vs hyperthyroidism
Hypothyroidism vs. Hyperthyroidism regulate the growth and development of an individual.

Symptoms of Hypothyroidism: Low thyroxin in the blood


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