Chapter 4 Enzymes Flashcards

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1
Q

Why are enzymes important

A

Enzymes are biological catalysts and interact with substrate molecules causing them to react at faster rates.

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2
Q

The role of enzymes in reactions

A

Living organism need to built and maintained, which involves synthesis of large polymers.
Enzymes are required for anabolic (building up) reactions and catabolic (breaking down) reactions.

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3
Q

Activation energy

A

The energy required for the reaction to start. Enzymes decrease the activation energy allowing reactions to occur more efficiently.

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4
Q

Lock and Key hypothesis

A

Enzymes have an active site which can only have one substrate fitting into it. The same way that only the right key will fit into a lock, only a specific substrate will fit the active site of an enzyme. When a substrate is bound to the active site it is called the enzyme substrate complex. Once reacted they are called the enzyme product complex.
The R- groups in the enzyme interact with the substrate creating temporary bonds.

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5
Q

Induced fit hypothesis

A

Enzymes active sites actually change shape slightly as the substrate enters - called induced fit hypothesis.
The initial interaction between enzymes and substrates is weak but this induces changes in the enzymes tertiary structure that strengthen binding, putting strain on the molecule. The weakens bonds, hence lowering activation energy.

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6
Q

Intracellular enzymes

A

Work within the cells that produce them
They have anabolic and catabolic pathways
anabolic - build complex molecules from simpler ones
catabolic - break down complex molecules to simpler ones.
E.g. catalase breaks down hydrogen peroxide ( toxic) into oxygen and water in the plant and animal tissues

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7
Q

Extracellular enzymes

A

Extracellular enzymes act outside the cells that produce and secrete them.
E.g.
Amylase - This is secreted by the salivary glands, pancreas, and small intestine to break down starch into maltose.
Trypsin - This is secreted by the pancreas into the small intestine to break down proteins into smaller polypeptides.

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8
Q

Temperature

A

As temperature increases, the rate of reaction increases. The molecules have more kinetic energy, causing more collisions and enzyme-substrate complexes
The maximum rate is reached at the optimum temperature. The optimum temperature is the temperature this enzyme works fastest at.
As temperature increases past the optimum, the rate of reaction decreases until the reaction stops. Too much kinetic energy causes the active site to change shape and the enzyme denatures.

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9
Q

Temperature coefficient

A

The temperature coefficient (Q10) is a value that shows how much the rate of reaction changes when the temperature is increased by 10°C.

Temperature 10°C = RoR at 10°C higher/ RoR at original.

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10
Q

pH

A

Below the optimum pH, the rate of reaction is low or zero. In acidic conditions, H+ ions break ionic/hydrogen bonds and denature enzymes.
The maximum rate of reaction is reached at the optimum pH. The optimum pH is the pH the enzyme works fastest at.
Above the optimum pH, the rate of reaction is low or zero. In alkaline conditions, OH- ions break ionic bonds or hydrogen bonds and denature enzymes.

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11
Q

Substrate concentration

A

As the substrate concentration increases, the rate of reaction increases. There are more substrate molecules to form more enzyme-substrate complexes.
As the substrate concentration increases further, the rate of reaction plateaus (levels off).This is the saturation point, which is when all active sites are occupied by a substrate and enzyme concentration becomes the limiting factor.

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12
Q

Enzyme concentration

A

As the enzyme concentration increases, the rate of reaction increases. There are more enzyme molecules to form more enzyme-substrate complexes.
As the enzyme concentration increases further, the rate of reaction plateaus (levels off). All substrate molecules available are being acted upon and substrate concentration becomes the limiting factor.

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