Enzymes (Unit 1) Flashcards

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1
Q

How can you increase the rate of a chemical reaction?

A

Temp, SA, concentration, catalyst

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2
Q

Cellular activity of all living things in controlled through?

A

Enzymes

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3
Q

Enzymes act as?

A

Catalyst to accelerate a reaction

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4
Q

Almost all enzymes are?

A

Proteins (tertiary and quaternary structures)

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5
Q

How are enzymes changed in a reaction?

A

Are not used up or permanently changed in the process, and do not change the products

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6
Q

Enzyme shape

A

Each is unique and will determine the reaction the enzyme will catalyze

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7
Q

Substrate

A

The specific reactant that an enzyme will bind with

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8
Q

Active site

A

The location on the enzyme where the substrate binds. This site “fits” the substance

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9
Q

Induced Fit Model

A

While each enzyme fits a specific substance, the enzyme is not rigid. Before the substrate binds, the active site changes its conformation to become even more precise in its ability to bind the substrate

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10
Q

How are enzymes named?

A

After their substrate. Sucrase breaks down sucrose, proteases break down proteins, lipases break down lipids

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11
Q

What must a reaction overcome in order to move forward?

A

Energy barrier known as the activation energy

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12
Q

How do enzymes work?

A

They alter the substrate or its environment which lowers the activation energy required to perform the reaction, so the reaction occurs at a faster rate

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13
Q

Factors Affecting Enzyme Activity

A

Cofactors and Coenzymes
Enzyme Inhibitors
Allosteric Regulation
Environmental Conditions

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14
Q

Cofactor

A

A non-protein group that binds to an enzyme and is essential for catalytic function. Are often metals/minerals - iron, copper, zinc, manganese

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15
Q

Coenzyme

A

Organic molecules that act as cofactors to enzymes. Usually vitamins

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16
Q

Types of Inhibitors

A

Competitive and Non-competitive

17
Q

Competitive Inhibitor

A

Chemicals that resemble an enzyme’s normal substrate and compete with it for the active site preventing the substrate from binding

18
Q

Non-competitive Inhibitor

A

Do not enter the active site, but bind to another part of the enzyme causing the enzyme to change its shape, which alters the active site so the substrate cannot bind

19
Q

Allosteric Regulators

A

Important molecules that function to control chemical activity in a cell. Inhibition or Activation

20
Q

Allosteric Inhibition

A

When the product of the reaction is in excess, an inhibitor will bind to the enzyme, changing its shape and stopping enzyme activity and production of the product

21
Q

Allosteric Activation

A

When the product is at low levels, an activator will bind to the enzyme, changing its shape to allow the substrate to bind to the enzyme, increasing the rate of reaction

22
Q

Environmental Conditions

A

Temperature, pH, Ionic Concentration

23
Q

Temperature

A

Extreme temperatures are very dangerous

24
Q

pH

A

Most like 6-8, or near neutral. pH outside of the normal range causes enzymes to lose their structure. Optimal pH range may change

25
Q

Ionic Concentration (salt ions)

A

Interferes with protein folding changing the shape of the enzyme