Enzymes Flashcards

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1
Q

Enzyme + type of protein

A

Biological catalysts that interact with substrate molecules to facilitate reactions.
Globular proteins

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2
Q

Substrate

A

A substance used or acted on by another process or substance.
A reactant in an enzyme-catalyzed reaction.
Complementary to the active site

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3
Q

Product

A

The final substance formed from the reaction facilitated by the enzyme.

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4
Q

Why are enzymes necessary to life

A

Enzymes help catalyze important reactions in metabolic pathways essential for life.

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5
Q

Anabolic reactions

A

Reactions that require energy that form larger, more complex molecules from smaller molecules.

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6
Q

Catabolic reactions

A

The breaking apart of molecules into smaller molecules to release energy

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7
Q

Digestion

A

The breaking down of chemicals in the body to a form that can be absorbed and used.

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8
Q

Metabolism

A

The sum of the chemical reactions that take place within each cell of a living organism and that provide energy for vital processes and for synthesizing new organic material.

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9
Q

Intracellular enzyme

A

Enzymes that act within cells: very sensitive to factors of rate of reaction.

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10
Q

Extracellular enzyme

A

Enzymes released from cells to break down these large (nutrient) molecules into smaller molecules that are taken in ie. for digestion.

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11
Q

Examples of intracellular enzyme

A

Catalase

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12
Q

Examples of extracellular enzyme

A

Amylase, Trypsin

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13
Q

Substrate and Product of Catalase

A

Catalyzes the decomposition of hydrogen peroxide to water and oxygen

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14
Q

Substrate and Product of Amylase

A

Amylose to Maltose

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15
Q

Substrate and Product of Trypsin.

A

Proteins to smaller peptides

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16
Q

Active site

A

Area of an enzyme with a shape complementary to a specific substrate, allowing the enzyme to bind with said substrate.

17
Q

Enzymes only work for one specific substrate as

A

The active site is specific to only the substrate that is complimentary to the enzyme’s active site.

18
Q

Lock and Key Hypothesis

A

Like a lock and a key, only a specific substrate will fit the active site of an enzyme.

19
Q

Induced-fit hypothesis

A

When a substrate molecule collides with an enzyme, if its composition is specifically correct, the shape of the enzyme’s Active Site will change so that the substrate fits into it and an Enzyme-Substrate Complex can form.

20
Q

The protein structures involved in making the shape of the active site

A

Tertiary structure

21
Q

Activation Energy

A

The energy required to initiate a reaction

22
Q

Rate of Reaction

A

The measure of how quickly it takes for an enzyme to convert all substrate into its products.

23
Q

Enzyme ____ Activation Energy

A

Reduces

24
Q

Factors Affecting the Rate of Reaction

A

Temperature
pH
Substrate Concentration
Enzyme Concentration

25
Q

Temperature and Enzymes

A
Higher temp= more kinetic energy
More collisions of substrate and active site
more ES complex formed
After optimum, temperature effects 3o
The active site is changed
26
Q

Temperature coefficient (Q10)

A

The measure of how much the r.o.r increases with a 10C temp. increase.
Usually 2 for enzyme controlled reaction

27
Q

Explain why Siamese cats are white with black tails, ears, paws, and faces.

A

The black fur helps conserve more heat in the extremities and so allows for the optimum temperature for enzymes.

28
Q

Why are enzymes so sensitive to pH

A

A slight change affects H bonds/ R groups ie. ionic bonds in 3o

29
Q

Substrate conc. and Enymes

A

Higher substrate conc. means more chance of active sites colliding with substrates.
More ES complexes formed
Until all substrates turned into products/Vmax

30
Q

Enzyme conc. and Enzymes

A

Higher enzyme conc. means more active sites colliding with substrates (higher chance).
More ES complexes formed
Until Vmax

31
Q

Vmax

A

Maximum initial velocity/rate of reaction of an enzyme

32
Q

co-factor/co-enzyme

A

Non-protein components that are necessary for the effective functioning of an enzyme.

33
Q

prosthetic group

A

Non-protein (metal ion) component of a conjugated protein.

34
Q

Enzyme inhibitor

A

Reduce the rate of an enzyme-catalyzed reaction by interfering with the enzyme in some way. This effect may be permanent or temporary.

35
Q

Competitive inhibitor

A

An inhibitor that competes with substrates to bind to an active site.
Still makes sure enzymes are re-usable so it does not affect V max.
reversible inhibitor

36
Q

Non-competitive inhibitor

A

An inhibitor that binds to the allosteric site of an enzyme, changing the shape of the active site.
Affects overall v-max.
Irreversible enzyme as the change of enzyme active site cannot be reversed

37
Q

Allosteric site

A

A site that allows molecules to inhibit enzyme activity by changing its active site shape. It’s different than the active site on an enzyme, where substrates bind.

38
Q

End Product Inhibition

A

The product of a reaction inhibits the enzyme required for the reaction.