focus chapter 6 (enzymes) Flashcards

1
Q

general properties of enzymes

A

o Biological catalysts
o Accelerate chemical reactions under physiological (mild) conditions
o Most are proteins
o Highly specific in their reaction and substrate
o Capacity for regulation
o Not changed or used up after a reaction

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2
Q

Oxidoreductases

A

 Can catalyze oxidation/reduction reactions
 Transfer electrons from one substance to another

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3
Q

Transferases

A

Transfer a functional group from one substance to another

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4
Q

Hydrolases

A

Help form two products through hydrolysis

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5
Q

Lyases

A

Non-hydrolytic addition or removal of groups from substrate

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6
Q

Isomerases

A

Intramolecule rearrangement (isomerization)

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7
Q

Ligases

A

New bonds with simultaneous breakdown of ATP

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8
Q

Translocases

A

Catalyze the movement of ions or molecules across membranes of their separation within membranes

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9
Q

Exergonic reactions have a

A

negative ΔG (free energy is released)…favorable

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10
Q

are endergonic or exergonic reactions favorable

A

exergonic

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11
Q

Endergonic reactions have a

A

positive ΔG (free energy input required)…unfavorable

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12
Q

A reaction is spontaneous if

A

 change in G is less than 0
 enzymes do not affect change in G

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13
Q

Thermodynamics

A

looks at standard free energy and tells you if the reaction will happen

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14
Q

kinetics

A

 How fast a reaction is happening
 Is effected by enzymes

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15
Q

energy diagrams of enzyme catalyzed reactions

A

o X-axis is reaction progress
 Time value
o Y-axis is free energy
 It tells you if the reaction is exergonic or endergonic
o The difference in heigh from the substrates and the products is the change in G for the reaction
o Catalyzed before transition state and uncatalyzed after

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16
Q

transition state

A

A molecular form that is no longer substrate but not yet product

17
Q

Enzymes facilitate the formation of

A

the transition state

18
Q

Activation energy

A

the energy required to form the transition state from the substrate

19
Q

Relate chemical kinetics to an understanding of how enzymes increase reaction rates

A

o Enzymes do not change the equilibrium of a reaction
o Enzymes decrease the activation energy, accelerating the reaction
o Enzymes decrease the time to reach the equilibrium

20
Q

Lock and key model

A

Substrate must perfectly fit the enzyme

21
Q

The induced fit model

A

When the substrate fits together with the enzyme, the enzyme itself will change to either join substrates together or break a substrate down

22
Q

the two main models describing enzyme-substrate interactions

A

lock and key model and the induced fit model

23
Q

key characteristics of enzyme active sites

A

o The active site is a three-dimensional cleft or crevice created by amino acids from different parts of the primary structure.
o The active site constitutes a small portion of the enzyme volume.
o Active sites create unique microenvironments.
o The interaction of the enzyme and substrate at the active site involves multiple weak interactions.
o Enzyme specificity depends on the molecular architecture at the active site.

24
Q

Explain the relationship between the transition state and the active site of an enzyme.

A

o Transition states are unstable arrangement of atoms that cannot be isolated.
o Transition state analogs mimics this arrangement, inhibiting the enzyme.
o Enzymes prefer to bind the transition state, because it represents the highest energy with the best binding.