Factors affecting Enzyme Actvivity Flashcards

1
Q

What is the importance of enzyme shape?

A

It determines the shape of the active site, which determines their function.
Any changes in the enzyme shape will affect the enzymatic yield

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2
Q

List the factors affecting enzyme activity

A

Temperature, pH, concentration of substrates, concentration of enzymes, presence of inhibitors

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3
Q

what is the preferred pH of enzymes

A

6-8
Pepsin in the stomach (~2)
Trypsin in the small intestine (~8)
If the pH is too low/high (outside it’s optimal range), the enzyme will denature

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4
Q

define “Denatured protein”

A

Protein that has lost its normal configuration and its ability to form an enzyme substrate complex

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5
Q

Temperature decrease

A

Lowering the temperature lowers the rate of activity (does not usually denature the enzyme)

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6
Q

What temperature do human enzymes start to denature

A

above ~40 degrees

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7
Q

Substrate concentration increases

A

Amount of product increases. The rate of product formation will usually increase too.
After a certain concentration, the rate won’t increase anymore, as all the enzymes are “saturated” with substrates and can’t work any faster

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8
Q

Temperature Increase

A

moderately, raises the rate of reaction
Largely, will denature the enzyme, which will lower the reaction rate

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9
Q

Substrate concentration decreases

A

The rate of product formation will generally decrease

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10
Q

Enzyme concentration increases

A

The more enzymes added, the more product produced
Rate of product formation increases

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11
Q

Enzyme concentration decreases

A

The less enzymes, the less products produced
The rate of product formation decreases

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12
Q

What does concentration limit

A

the overall rate of reaction
Rate will only level off if you run out of substrate (usually not the case)

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13
Q

What are inhibitors

A

molecules that bind to the enzyme in some way to prevent/reduce the rate of substrate binding to the enzyme

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14
Q

competitive inhibition

A

Molecule that looks like the substrate can compete for a place where the substrate binds to the enzyme, slowing down the reaction rate
The inhibitor binding to E can be reversible or irreversible
More inhibitors = lower reaction rate = lowering products made

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15
Q

Non-competitive Inhibition

A

Inhibitor binds to another place on the enzyme, not on the active site (may look different from the substrate)
Binding causes enzyme to change shape at the active site so substrate cannot bind
Binding may be reversible or non-reversible
Also known as “allosteric” inhibition

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16
Q

Inhibition can also be chemicals introduced into the system from outside

A

Can act as medicines or poisons
Ex. Penicillin, a medicine that kills bacteria, works by binding irreversibly to the enzyme that makes bacterial cell walls
HCN (hydrogen cyanide), lethal irreversible inhibitor of enzyme action in humans

17
Q

heavy metals

A

Lead and other heavy metals (mercury, cadmium) are non-competitive inhibitors that cause poisoning when they bind irreversibly to enzymes and make them denature

18
Q

reversible imhinition

A

often used as a normal way of slowing down metabolic pathways

19
Q

Thyroxin

A

Thyroid hormones (T4 and T3) increase the metabolic rate of cells
They stimulate all organs to metabolize at a faster rate
Production of thyroxin(e) requires iodine