Enzymes Flashcards

1
Q

Chemical agents that speed up chemical reactions without being consumed

A

Catalysts

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2
Q

Chemical agents that speed up chemical reactions without being consumed (Catalysts in biomolecules)

A

Enzymes

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3
Q

Chemical reaction involves

A

breaking or forming a bond

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4
Q

Changing one molecule into another generally involves

A

contorting the starting molecule into a highly unstable state before the reaction can proceeed

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5
Q

To reach the contorted state, molecules need to absorb

A

Energy — Activation Energy (supplied with thermal energy)

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6
Q

What does the energy do?

A

The energy accelerates the reactant molecules and collides more often causing the breakage of a bond.

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7
Q

When molecules absorb enough energy,

A

the reactant molecule goes into an unstable condition called a transition state

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8
Q

What comes after the transition state?

A

Atoms settle into more stable bonding arrangement as energy is released into their surroundings. Molecules return to the stable shape and lower energy.

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9
Q

[ToF] Can too much heat kill the cell?

A

Ye

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10
Q

How does an enzyme catalyze a reaction?

A

by lowering the Energy Activation barrier, enabling the reactant molecules to absorb enough energy to reach the transition state even at moderate temperatures.

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11
Q

The reactant an enzyme acts on

A

Substrate

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12
Q

Forms after enzymes bind to its substrate

A

Enzyme-substrate Complex

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13
Q

Summary of catalytic action of enzymes

A

Enzyme + Substrate <-> Enzyme-substrate complex <-> Enzyme + products

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14
Q

Typically a pocket or groove on the surface of the enzyme where catalysis occurs

A

Active site

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15
Q

Formed by only a few amino acids, with the rest of the protein molecule providing a framework that determines the shape of the active site

A

Active site

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16
Q

[ToF] Enzymes are stiff structures locked into a given shape

A

False

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17
Q

The tightening
of the binding after initial contact; the shape change that makes the active site fit even more snugly around the substrate

A

Induced fit

18
Q

Process of catalysis

A
  1. Substrate enters the active site, enzyme changes shape to fit it
  2. Substrates are held in the active site by weak interactions (hydrogen bonds/ionic bonds)
  3. Active site lowers activation energy and speeds up the reaction
  4. Substrates are converted into products (wahhaha binubugbog)
  5. Products are released
  6. Active sites are available for more molecules
19
Q

Components of an enzyme

A

Cofactor (co-enzyme, metal ions, prosthetic groups), Apoenzymes, Holoenzymes

20
Q

Nonproteins that help mediate enzymatic reactions. They serve as nucleophiles, mediate covalent catalysis, form electrostatic interactions with the substrate, and stabilize the transition state.

A

Cofactors

21
Q

Bind to the enzyme and remove electrons/protons/chemical groups from the substrate

A

Cofactors

22
Q

Loosely-bound organic cofactors that may assume the role of hydrogen acceptors [Nicotinamide adenine dinucleotide (NAD), Adensonine Triphosphate (ATP)]

A

Co-enzyme

23
Q

Tightly-bound inorganic/organic cofactors (Heme, biotin, flavin, iron sulphides, copper, and ubiquinone)

A

Prosthetic groups

24
Q

Inorganic such as the metal atoms zinc, iron, and copper in ionic form

A

Metal ions

25
Q

No associated cofactors

A

Apoenzymes

26
Q

Complete enzymes

A

Holoenzymes

27
Q

Model that suggests that enzymes are rigid (cannot change) [maling model lmfaoo]

A

Lock and key model

28
Q

Suggests that enzymes are flexible, and can change to accommodate substrates

A

Induced fit model

29
Q

Characteristics of Enzymes

A
  • Specific
  • Reusable (into the same chemical reactions)
  • Flexible
30
Q

Limit catalysts/enzymes and prevent them from doing their jobs

A

Inhibitors

31
Q

In which an inhibitor competes with substrate for binding to an active site. When it occupies said active site, it forms an enzyme-inhibitor complex and the enzyme cannot react until the inhibitor dissociates.

A

Competitive Inhibition

32
Q

They have a structure similar to the substrate, but they are unreactive.

A

Competitive Inhibitors

33
Q

Example of competitive inhibitor

A

Statins - a class of drugs that reduces cholesterol levels. They are inhibitors of the enzyme HMG-CoA
reductase. HMG-CoA reductase is the enzyme that synthesizes cholesterol from lipids

34
Q

In which an inhibitor binds to an enzyme at a location other than the active site. In some cases, these inhibitors physically block the normal active site or change the shape of the enzyme molecule entirely, deforming the active site. Involves negative feedback.

A

Noncompetitive inhibition

35
Q

In which inhibitors bind only to the substrate-enzyme complex. Common in reactions involving two or more substrates or products. Products leave the active site less easily, slowing the reaction

A

Uncompetitive Inhibition

36
Q

Factors affecting enzyme activity

A

Temperature, pH, substrate concentration, enzyme concentration

37
Q

Relationship between Enzyme Activity and Temperature

A

The higher the temperature, the faster the reaction (substrates and active sites collide more frequently)

38
Q

Relationship between Enzyme Activity and pH

A

The optimal pH value for enzymes is between pH 6-8.

Exceptions include pepsin that works at a low pH, and trypsin in more alkaline parts of the intestine that are more denatured.

39
Q

Relationship between Enzyme Activity and Substrate Concentration

A

Increasing substrate concentration also increases the rate of reaction until all enzymes have bound

40
Q

Relationship between Enzyme Activity and Enzyme Concentration

A

Increasing enzyme concentration will speed up the reaction as long as there is substrate available to bind to. Once all of the substrate is bound, the reaction will no longer speed up because additional enzymes will have nothing to bind to.