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PHARM 113 > ENZYME PART 2 > Flashcards

ENZYME PART 2 Flashcards

1
Q

Catalytic mechanisms

A

Acid-base catalysis
Nucleophilic catalysis
Elctrophilic catalysis
Catalysis by proximity and orientation
Preferential transition state binding

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2
Q

Acid-base catalysis

A

Proton donation and acceptor
Histidine

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3
Q

Nucleophilic catalysis

A

Nucleophile (enzyme)
Electrophile (substrate)

Promote substitution reaction

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4
Q

Serine Proteases: Catalytic Triad

A

Ser His Asp

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5
Q

Ser

A

Nucleophile; Nucleophilic catalyst
Form covalent bond

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6
Q

His

A

Acid base catalyst

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7
Q

Asp

A

Stabilizes histidine

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8
Q

Electrophilic catalysis

A

Nucleophile: Substrate
Electrophile: Enzyme
Elimination

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9
Q

Electrostatic Catalysis

A

Binding substrate excludes H2O from the active site
Local dielectric constant active site resembles that in an organic solvent
Ionic interactions

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10
Q

Catalysis by proximity and orientation

A

Enzyme attract substrate in certain orientation to react with cosubstrate

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11
Q

Preferential transition state binding

A

Transition state has higher binding affinity than the substrate

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12
Q

Regulation of activity

A

Coordination of numerous metabolic processes in the cell
Respond to changes in its environment
Grow and differentiate all in an orderly manner

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13
Q

Enzyme types based on regulation

A

Constitutive
Inducible

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14
Q

Constitutive

A

Produced all the time
Healthy state or normal state

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15
Q

Inducible

A

Produced only when needed or in the presence of substrate

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16
Q

Regulatory mechanisms

A

Feed forward
Positive feedback
Negatuve feedback
Up regulation
Down regulation
Allosteric regulation

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17
Q

Allosteric site

A

Any part of the enzyme but not active site
Alters the acitivity of the enzyme

18
Q

Monod, Wyman, Chageux (MWC) Model

A

Symmetrical model
One step activation or deactivation

19
Q

Koshland, Nemethy, Filmer (KNF) Model

A

One subunit is active and the other one is not
Two step activation

20
Q

Regulation by covalent modification

A

Protein kinase - activate the enzyme
Protein phosphatase - deactivate the enzyme

21
Q

Regulation by modular proteins

A

Convert inactive enzyme into active enzyme
Promotes the phosphorylation of other protein or other enzymes

22
Q

Factors affecting enzymatic activity

A

Temp.
pH
Substrate conc

23
Q

Michelis-Menten Model

A

Applies only to enzymes that dont have multiple binding sites and whose Km is higher than the total enzyme concentration

24
Q

Km

A

Substrate conc at Vmax/2
[E][S]/[ES]

25
Q

Linewaever-Burk Plot

A

1/Vo=(Km/Vmax)1/[S] + 1/Vmax

26
Q

Enzymes are highly efficient

A

10^3 - 10^8 times faster than uncatalyzed reactions

27
Q

Product turnover per enzyme molecule

A

100-1000/sec

28
Q

Kcat=Vmax/[E]T

A

Number of processes that each active site catalyzes per unit of time

29
Q

Kcat/Km

A

Measure of the catalytic efficiency of the enzyme

30
Q

Measuring reaction velocity

A

V=delta[P]/delta[Time] or delta[S]

31
Q

Competitive inhibitors

A

Binds in free enzymes to form EI
same Vmax
High Km
High slope

32
Q

Uncompetitive Inhibitors

A

Binds ES complex to form ESI
Low Vmax
Low Km
Same slope

33
Q

Mixed Inhibitors

A

Binds free enzyme and ES complex
Low Vmax
High Km
High slope

34
Q

Mixed Noncompetitive

A

Binds free enzyme allosteric to form EI
Low Vmax
Same Km
High slope

35
Q

Enzymes as drugs

A

Oncolytic agents
Anticoagulant
Enzyme replacement therapy

36
Q

Oncolytic agents

A

L-asparagine
Neuraminidase

37
Q

Anticoagulant

A

Tissue plasmin activator
Streptokinase

38
Q

Enzyme replacement therapy (ERT)

A

Collagenase
Papain
Trypsin and chymotripsin

39
Q

Enzymes used in clinical diagnosis

A

Present in highest conc
Present at low level
Used as reagent

40
Q

Enzymes present in highest concentration

A

Has systemic functional role
Thrombin in blood coagulation

41
Q

Enzymes present at low level

A

No systemic functional role
Indicators of disease of organs and tissues

42
Q

Enzymes used as reagent

A

Creatinase, cholesterol oxidase, glucose peroxidase

PHARM 113 (5 decks)

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