1.7 Enzymes Flashcards

To understand 1.7 enzymes

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1
Q

What are enzymes?

A

Enzymes are proteins that act as biological catalysts by accelerating chemical reactions.

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2
Q

How many different enzymes are typically found in a living cell?

A

About 4000 enzymes

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3
Q

What is a catalyst?

A

A substance that speeds up a reaction without being consumed; in biological systems, enzymes act as catalysts.

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4
Q

What is the active site of an enzyme?

A

The location where the substrate binds, usually a pocket or groove formed by the enzyme’s tertiary structure.

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5
Q

Describe the lock-and-key method

A

A model explaining how specific substrates (keys) fit into specific enzymes (locks) for catalysis.

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6
Q

What is the induced-fit method

A

Instead of the enzyme’s active site being a perfect fit for the substrate from the start, the enzyme changes its shape slightly when the substrate binds. This adjustment helps the enzyme bind more tightly and increases the enzyme’s range of specificity, allowing it to interact with multiple substrates. As a result, one enzyme can work on a variety of substrates, making it more versatile.

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7
Q

What is the enzyme-substrate complex?

A

The temporary complex formed when an enzyme binds to its substrate(s) before converting them into products.

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8
Q

What are cofactors?

A

Non-protein groups, often metals, that bind to enzymes and are essential for their catalytic activity.

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9
Q

What are coenzymes?

A

Organic helpers, usually from vitamins, that assist enzymes.

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10
Q

What factors affect how enzymes work?

A

Substrate concentration, temperature, and pH (acidity).

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11
Q

What is competitive inhibition?

A

When an inhibitor with a structure similar to the substrate occupies the active site, stopping the substrate from binding. The effect can be reversed by increasing substrate concentration

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12
Q

What is noncompetitive inhibition?

A

The inhibitor does not have a structure like the substrate, and it binds to another part of the enzyme. It changes the shape of the enzyme and active site so that the substrate cannot fit the altered active site. No reaction occurs, and the effect cannot be reversed by adding substrate/increasing substrate concentration.

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13
Q

What is allosteric regulation?

A

A method used by cells to control enzyme activity. Is it when a molecule binds to an enzyme and changes its shape, affecting its activity

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14
Q

What can happen if an enzyme is missing or defective?

A

It can lead to serious problems, like metabolic disorders, where the body can’t break down certain substances. For example, a missing enzyme in lactose intolerance prevents proper digestion of lactose, causing symptoms like bloating and cramps.

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14
Q

What is feedback inhibition?

A

A way to control reactions where the end product stops an earlier step from happening if there’s too much

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15
Q

Give an example of feedback inhibition

A

Isoleucine can stop the enzyme that makes it when there’s enough of it

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16
Q

What does the enzyme lipase do?

A

It helps break down lipids (fats) into smaller parts.

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17
Q

What reaction does sucrase catalyze?

A

It breaks down sucrose (sugar) into glucose and fructose.

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18
Q

What is enzyme specificity?

A

Each enzyme only works with a specific substrate or a group of similar substrates.

19
Q

How do temperature changes affect enzymes?

A

Too high or too low temperatures can change an enzyme’s shape, making it less effective.

19
Q

Why do enzymes have a unique shape?

A

Their shape determines which substrate they can bind to and what reaction they can speed up.

20
Q

What happens to enzyme activity if the pH level changes too much?

A

Enzymes have an optimal pH for maximum activity. Extreme pH levels can denature (change the shape of) the enzyme, reducing its activity.

21
Q

How can the concentration of substrate affect enzyme activity?

A

More substrate can increase the reaction rate until the enzyme is saturated.

22
Q

What is saturation level in enzyme reactions?

A

The point where all enzyme active sites are occupied by substrate, and adding more substrate doesn’t increase the reaction rate.

23
Q

What is an example of an enzyme with a low pH optimum?

A

Pepsin, which works best at a pH of 1.5 in the stomach

23
Q

What role do antibiotics play regarding enzymes in bacteria?

A

They often inhibit bacterial enzymes, preventing bacteria from growing.

23
Q

What is irreversible inhibition?

A

It’s when an inhibitor permanently attaches to an enzyme, stopping it from working. This type of inhibition is called noncompetitive inhibition because it changes the enzyme’s shape, so the substrate can’t react with it anymore.

23
Q

When an inhibitor permanently binds to an enzyme, stopping it from working.

A

Cyanide is a toxic irreversible inhibitor. It binds to an enzyme needed for cellular respiration, preventing cells from using oxygen. This is dangerous because it stops energy production in cells, which can be fatal.

23
Q

What is the typical pH optimum for most enzymes?

A

Around 7, which is close to the pH of cellular contents.

24
Q

What is denaturation in enzymes?

A

It’s when the enzyme’s structure unravels due to high temperatures, causing it to lose function.

24
Q

How do enzymes from organisms in cold regions differ?

A

They have lower temperature optima, functioning best near 0°C. This allows them to maintain activity in cold environments where other enzymes might be inactive, ensuring essential biological processes continue despite low temperatures.

24
Q

What is an example of an enzyme with a high pH optimum?

A

Trypsin, which operates best at about pH 8 in the intestine

24
Q

How does temperature affect enzyme activity?

A

Generally, as temperature increases, reaction rates increase until enzymes begin to denature.

24
Q

What is the typical temperature range for peak enzyme activity?

A

Between 40°C and 50°C, where kinetic motion is high but denaturation hasn’t occurred.

24
Q

What is lactose intolerance?

A

A condition where individuals do not produce enough lactase, leading to symptoms like nausea and cramps after consuming lactose.

24
Q

How do enzymes improve laundry detergents?

A

They help remove stains better at lower temperatures and with less scrubbing. They are a mix of proteases (for proteins), lipases (for fats), and amylases (for starches).

24
Q

What is lactase?

A

An enzyme that breaks down lactose into glucose and galactose, important for digestion in individuals without lactose intolerance.

24
Q

What happens to enzyme activity above 60°C?

A

The activity drops to zero as the enzyme denatures.

24
Q

What happens to digestion without sufficient water?

A

Improper temperature and pH lead to inefficient digestion, impaired nutrient absorption, and affected waste removal, potentially causing discomfort and health issues.

25
Q

What role does water play in enzymatic reactions during digestion?

A

Water is involved in hydrolysis, which is necessary for breaking down complex molecules into simpler forms.

25
Q

Why is water necessary for digestion?

A

Water acts as a solvent, helping to break down food, transport nutrients, and facilitate enzymatic reactions.

25
Q

Why is it important for the human body to maintain a proper temperature?

A

Proper temperature ensures enzyme activity, metabolic processes, and overall bodily functions work efficiently at 37°C

26
Q

What enzymes are in contact lens solution?

A

Proteases and lipases are added to get rid of dirt

27
Q

What enzymes are in meat tenderdiser?

A

Protease can be added to tough cuts of meat to make it more tender

27
Q

What are some uses of enzymes in industry?

A

Enzymes have many industrial and commercial uses, including in food production, cleaning products, and biofuels.

28
Q

What are inhibitors?

A

Inhibitors are substances that decrease or block enzyme activity by binding to the enzyme, either at the active site (competitive inhibitors) or at another site (noncompetitive inhibitors).