Enzymes Flashcards

(32 cards)

1
Q

Activation Energy

A

The minimum amount of energy needed for a reaction to happen

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2
Q

Active Site

A

A specific region on an enzyme where the substrate binds and the reaction takes place

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3
Q

Amylase

A

An enzyme that catalyses the extracellular breakdown of starch

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4
Q

catalase

A

An enzyme that catalyses the intracellular breakdown of hydrogen peroxide into oxygen and water

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5
Q

Coenzyme

A

A type of cofactor that is bound loosely o an enzyme with weak interactions

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6
Q

Cofactors

A

A non-protein molecule that is needed for the effective functioning of an enzyme

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7
Q

Competitive Inhibitor

A

A molecule which binds to the active site of an enzyme and prevents the substrate from binding

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8
Q

End Product inhibition

A

A method of enzyme inhibition where the product f an enzyme controlled reaction can bind to the enzyme and prevent it from workin

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9
Q

Enzyme

A

A biological catalyst used to speed up the rate of biochemical reactions without being used up or permanently altered

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10
Q

Enzyme-Product Complex

A

The temporary complex formed after the enzyme has catalysed the reaction but before the products have left the active site of the enzyme

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11
Q

Enzyme Substrate Complex

A

The temporary complex formed when th substrate binds to the active site of the enzyme

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12
Q

Extracellular reaction

A

A reaction that occurs outside of cells

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13
Q

Inactive Precursor

A

An inactive form of an enzyme that cannot carry out its function until it is activated

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14
Q

Induced fit hypothesis

A

A model of enzyme action that describes how once a specific substrate binds to the active site; the enzyme undergoes subtle conformational changes to fit the substrate better

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15
Q

Intracellular Reaction

A

A reaction that occurs inside the cells

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16
Q

Lock and Key hypothesis

A

A model of enzyme action that describes how the enzyme will only fit a substrate that has the correct complimentary shape to the active site

17
Q

Metabolism

A

The sum of all the chemical reactions taking place in a cell

18
Q

Non-Competitive Inhibitor

A

An inhibitor which binds to a different part of an enzyme known as the allosteric site and prevents the enzyme from functioning

19
Q

Prosthetic group

A

A type of cofactor that is bound tightly to an enzyme with strong interactions

20
Q

Substrate Specificity

A

The ability of an enzyme to catalyse only a specific reaction or set of reactions which have substrates complementary to the active site of the enzyme

21
Q

Trypsin

A

An enzyme that catalyses the extracellular breakdown of proteins

22
Q

Enzymes Notes

A
  • Biological catalysts
  • Globular proteins
  • have a specific tertiary structure
  • Catalyses metabolic reactions
  • Lowers the activation energy of reaction
23
Q

Effect of Temperature on Enzymes

A

As the temperature increases the kinetic energy does to. This means the substrate and the enzymes move around faster. The substrate and active site collide more often so Enzyme Substrate Complexes form which increases the rate of reaction.
Heat makes the molecules vibrate so the the weaker and ionic bonds break. The tertiary structure of the enzyme and active site changes shape so the substrate no longer first then the enzyme denatures

24
Q

Effect of PH on Enzymes

A

Enzymes have an optimum PH,where the rate of reaction is highest. The hydrogen and ionic bonds that hold the tertiary structure in place get broken. This alters the tertiary structure which denatures the enzyme since the substrate no longer fits the site and the enzyme substrate complex cannot form

25
Effect of Enzyme Concentration on Enzymes
There are more active sites so it is easier for the substrate to collide with the active site so more name substrate complexes form increasing the rate of reaction.
26
Effect of Substrate Concentration on Enzymes
There are more substrates to collide with the active site so more enzyme substrate complexes form which increases the rate of reaction
27
Enzyme Regulation
- Enzymes can be activated by coenzymes - Enzymes can b inactivated by inhibitors - Inhibitors slow or stop enzyme activity - Inhibitors can be ir/rversible
28
Competitive Inhibition
- have similar shape to the substrate so they fit in the active sites - The inhibitor blocks the active site - The activity of the enzyme is decreased
29
Non-Competitive Inhibitors
- Binds at the allosteric site - a location other than the active site - The binding causes the tertiary structure to change shape - The substrate cannot bind to the active site
30
Irreversible Non-Competitive Inhibitors
- Cannot be removed from the enzyme they are attached to
31
End Product Inhibition
- The product of the reaction acts as an inhibitor for the enzyme that produces - Serves as negative feedback
32
Cofactors
- A non protein compound required for the enzymes activity to occur - three types: activators, coenzymes and prosthetic groups - Coenzymes are organic factors which do not bind permanently, they facilitate the binding of the substrate - Activators are inorganic metal ions which temporarily binds to the inactive precursor enzyme and alters its active site - Prosthetic Groups are permanently attached to the enzyme