Enzymes Flashcards

(33 cards)

1
Q

What is a ribozyme?

A

An RNA molecule that can catalyze a biochemical reaction

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2
Q

What is an Abzyme?

A

A product produced in the lab by attaching an antibody to the active site structure isolated from an enzyme

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3
Q

What’re the two models for enzyme structure and function?

A
  • Lock/Key

- Induced Fit

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4
Q

What nonprotein components are essential for enzyme activity?

A
  1. Prosthetic groups: Nonroteiin organic structures tightly bound to enzyme ex. Heme in cytochrome C
  2. Coenzymes: Less tightly bound substance frequently derived from vitamins
  3. Cofactors: Metal ions or simple organic molecules
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5
Q

What are the classifications of enzymes?

A
  • Oxidoreductase
  • Tranferase
  • Hyrdolase
  • Lyase
  • Isomerase
  • Ligase
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6
Q

What type of reaction is catalyzed by an Oxidoreductase?

A

Redox rxns (Addition/removal of e-)

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7
Q

What type of reaction is catalyzed by a Tranferase?

A

Transfer of a specific group (phosphorylation, etc)

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8
Q

What type of reaction is catalyzed by a Hydrolase?

A

Bond breakage via H20

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9
Q

What type of reaction is catalyzed by a Lyase?

A

Bond breakage w/h out water

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10
Q

What type of reaction is catalyzed by an Isomerase?

A

Formation of an Isomer (ex group switching trans/cis)

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11
Q

What type of reaction is catalyzed by a Ligase?

A

Bond formation (ex carboxylation)

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12
Q

How does pH affect pH?

A
  • Enzymes operate optimally about some particular pH. Activity drops off in a bell shaped curve around that pH
  • Due to chaired groups at active sites or salt bridges =becoming titrated
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13
Q

Ho does temperature affect enzyme activity?

A
  • there is an optimal temperature for enzyme activity

- Temperature increases kinetic activity until a certain point at which the protein starts to denature

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14
Q

What are isozymes?

A

Enzymes from the same species which have the same activity, but differ in chemical structure and kinetic properties

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15
Q

Heat is the Michealis-menton equation?

A

V = Vmax[S] / [S] + Km

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16
Q

What is the reaction velocity at very low [S]?

A

V = Vmax[S] / Km

17
Q

What is the reaction velocity at very high [S]?

18
Q

How does enzyme concentration affect Km?

19
Q

How is enzyme Km related to binding affinity?

A

Smaller Km, Higher affinity

20
Q

How are reaction rates related to dissociation contants?

21
Q

What is the line weaver-Burk equation?

What is the slope?

What is it’s usefulness in medicine?

A

1/V = Km/Vmax x 1/[S] x 1/Vmax

Slope = Vmax

Used to identify inhibitors

22
Q

What is the equation for the Eddie-Hofstra plot?

A

V = {-Km(V)} / [S]

23
Q

What are the two types of inhibitors, and how do they affect Km and Vmax?

A

Irreversible: Removes some enzyme from reaction mixture; only affects Vmax

Reversible: Can affect either or both Km or Vmax

24
Q

What is an example of beneficial irreversible inhibition?

A

Penicillin for inhibiting glycopeptuide transpeptidase in staph. Aureus

25
What are the three types of reversible inhibitors?
1. Competitive 2. Uncompetitive 3. Noncompetitive
26
What is an example of competitive inhibition?
Rate-limiting step for Cholesterol biosynthesis Reduction of 3 hydroxymethylglutaryl Coa to Mevalonate and CoAsh
27
What is an example of noncompetitive inhibitors?
Lead poisoning causing anemia
28
What is an example of uncompetitive inhibitors?
Lithium inhibition of Inositol phosphatase | Manic depression
29
How are allosteric enzyme regulated?
- Either inhibited or activated by effectors binding to a site other than the active site
30
What are the states of an allosteric enzyme?
R State - More Active (relaxed) T State - Less active (Taut)
31
What is an example of allosteric regulation?
Regulation of aspartame transcarboxylase to produce N-Carbamoyl Aspartate
32
How is K calculated for Allosteric enzymes?
K = [S]^n x [Vmax - V] / V
33
When is a lineweaver Burke plot linear for an allosteric enzyme?
When n = 1