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Biochemistry > Enzymes > Flashcards

Enzymes Flashcards

1
Q

Conjugated proteins
Catalyst/Speed up or hasten biochemical reaction
Very efficient and effective
Highly specific

A

Enzymes

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2
Q

Enzymes accelerate chemical reactions by decreasing

A

the energy of activation of the reaction

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3
Q

Protein portion of enzyme

A

Apoenzyme

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4
Q

Non protein portion of enzyme

A

inorganic e.g. metal ions -> co factors

organic e.g. NAD, FAD, FMN -> coenzyme

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5
Q

Inorganic non protein portion of enzyme

A

Cofactors

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6
Q

Organic non-protein portions

Usually vitamins

A

Coenzyme

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7
Q

Apoenzyme (protein) + Cofactor/Coenzyme (nonprotein)

A

Holoenzyme

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8
Q

Amount of energy required to produce a transition state and bring about a reaction

A

Energy of activation (Ea)

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9
Q

Enzymes that catalyze oxidations and reductions

A

Oxidoreductases

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10
Q

Enzymes that catalyze transfer of moieties such as glycosyl, methyl, or phosphoryl groups

A

Transferases

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11
Q

Enzymes that catalyze hydrolytic cleavage of C-C, C-O, and other covalent bonds

A

Hydrolases

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12
Q

Enzymes that catalyze CLEAVAGE of C-C, C-O and other COVALENT bonds by

Atom elimination
Generation of double bonds

A

Lyases

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13
Q

Enzymes that catalyze GEOMETRIC or STRUCTURAL changes within a molecule

A

Isomerases

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14
Q

What is the action of glutaminase enzyme?

A

Hydrolytic cleavage
Hydrolase

Catalyzes glutamine to glutamate

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15
Q

Two sites of enzymes

A

Active site

Substrate recognition site

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16
Q

The substrate can bind to the enzyme to form an

A

Enzyme-Substrate Complex

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17
Q

Substrate binds to the enzyme at the

A

active site

18
Q

When the reaction is complete the products are released and the enzyme can be used again

The result:

A

reaction product

19
Q

Substrate + Active Site = ES Complex

Substrate perfectly fits on active site

A

Rigid Template Model
(Emil Fischer)
Lock and Key Model

20
Q

As substrate binds, enzyme undergoes a confirmational change that repositions amino acids in the active site and increases interactions with the substrate

A

Induced Fit Model
(Daniel Koshland)
Flexible Fit Model

21
Q

Active site assumes shapes that are complementary to that of the substrate only after the substrate is bound

A

Induced Fit Model
(Daniel Koshland)
Flexible Model

22
Q

Is the velocity approached at a saturating concentration of the substrate

A

Vmax

23
Q

Is the concentration of the substrate required to produce 1/2 Vmax

A

Km

24
Q

Km =

A

Km = 1/2 Vmax

25
Q

Relates the initial velocity to substrate concentration [S] and maximum velocity

A

Michaelis Menten Equation

26
Q

Initial velocity is directly proportional to

A

Vmax

27
Q

Initial velocity is inversely proportional to

A

Km

28
Q

This equation describes how reaction velocity varies with substrate equation

sigmoidal

A

Michaelis-Menten Equation

29
Q

vi =

A

vi initial velocity= Vmax / Km

30
Q

is the S at half maximum velocity

is a measure of the affinity of an enzyme for its substrate

A

Km

31
Q

Describes the catalytic aspect of enzyme action

Reveals the turnover number

A

Vmax

32
Q

This is a double reciprocal plot used to calculate Km and Vmax

as well as to determine the mechanism of action of enzyme INHIBITORS

A

Lineweaver-Burke plot

33
Q

Derived from the reciprocal of the Michaelis Menten equation

Gives the equation of a straight line

A

Lineweaver-Burke Plot

34
Q

Interferes with active site of enzyme so substrate cannot bind

A

Competitive inhibition

35
Q

Changes shape of enzyme so it cannot bind to substrate

A

Noncompetitive inhibition

36
Q

The structure of the inhibitor resembles the substrate

A

Competitive inhibition

37
Q

Km increases

Vmax constant

A

Competitive inhibition

38
Q

Competitive inhibitions aims to

A

overcome increased concentration of substrate

39
Q

Km constant

Vmax decreases

A

Non Competitive inhibition

40
Q

Aim of non competitive inhibition is

A

Reversible or irreversible binding depending on whether the inhibitor binds temporarily or indefinitely

Biochemistry (32 decks)

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