05.0 Enzymes - AI testing Flashcards

1
Q

What are enzymes?

A

Biological catalysts made of proteins

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2
Q

What is a catalyst?

A

Substance that increases the rate of a chemical reaction without being changed itself

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3
Q

What do enzymes control?

A

Specific reactions that make life possible

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4
Q

How do enzymes work?

A

They lower the activation energy required for a reaction to occur

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5
Q

What are substrates?

A

The beginning molecule in the reaction that binds to the enzyme at the active site

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6
Q

What is the active site of an enzyme?

A

Highly specific region where substrates bind

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7
Q

What is an enzyme-substrate complex?

A

The formed complex when substrates bind to the enzyme

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8
Q

What happens to products after a reaction?

A

They can be released, allowing the enzyme to perform another reaction

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9
Q

How many reactions can enzymes perform per second?

A

Hundreds, with some enzymes like catalase performing tens of millions

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10
Q

What factors affect enzyme activity?

A

Amount of substrate, temperature, pH, presence of coenzymes or cofactors, inhibitors, heavy metals, availability of energy

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11
Q

What is saturation in enzyme kinetics?

A

When all active sites of the enzyme are occupied due to increased substrate

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12
Q

What is the relationship between enzymes and cofactors?

A

Most enzymes require cofactors to work, which can be inorganic ions or non-protein organic molecules

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13
Q

What are prosthetic groups?

A

Non-protein organic molecules that are permanently bound to enzymes, e.g. heme in catalase

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14
Q

What are coenzymes?

A

Organic molecules that react with the substrate and can be released by the enzyme, e.g. ATP, NAD

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15
Q

What is enzyme specificity?

A

Enzymes usually catalyze only a particular reaction

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16
Q

What is an example of enzyme specificity?

A

Invertase catalyzes the hydrolysis of sucrose to glucose and fructose

17
Q

What is irreversible inhibition?

A

When a covalent bond is formed between the inhibitor and the enzyme, not easily broken

18
Q

What is reversible inhibition?

A

When the inhibitor molecule binds through attractive forces, affecting enzyme function

19
Q

What is a competitive inhibitor?

A

Blocks the substrate from entering the active site

20
Q

What is a non-competitive inhibitor?

A

Does not bind to the active site but affects enzyme function by binding elsewhere

21
Q

How does temperature affect enzyme activity?

A

Increase in temperature increases molecular movement, leading to more frequent collisions with active sites

22
Q

What happens if temperature exceeds the optimum for an enzyme?

A

The enzyme will begin to denature

23
Q

What is the difference between partially denatured and completely denatured enzymes?

A

Partially denatured enzymes can regain their shape after cooling; completely denatured cannot function correctly again