Enzymes Flashcards

1
Q
  1. What is the definition of enzymes?
A

Complex biological molecules, entirely protein
Acts as a biological catalyst via binding and chemically transforming other molecules
Increases rate of chemical reaction
Specific to their actions with only one substrate

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2
Q
  1. What is a cofactor
A

Helper molecules that assist in the biochemical transformation

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3
Q
  1. What is an organic cofactor called?
A

Coenzyme > prosthetic or co-substrate group

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4
Q
  1. What are the important coenzymes?
A

ATP
NAD
FAD
coenzyme A

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5
Q
  1. What is the difference between an apoenzyme and a holoenzyme?
A

Apoenzyme: no cofactor bound > inactive form
Holoenzyme: apoenzyme + co factor bound > active form

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6
Q
  1. What is the active/catalytic site of an enzyme?
A

location in which the substrate binds > complex leads to conformational changes

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7
Q
  1. How many classes of enzymes do exist?
A
  1. Oxidoreductase
  2. Isomerase
  3. Hydrolase
  4. Transferases
  5. Translocases
  6. Ligases/ Synthase
  7. Lyases
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8
Q
  1. What is an exergonic and endergonic reaction?
A
  • Exergonic: energy release
  • Endergonic: energy absorb
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9
Q
  1. For what is the Michaelis-Menten formula/equation used for?
A

determines the catalytic activity of enzymes via rate analysis at a particular substrate concentration

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10
Q
  1. What happens in the catalytic reaction of the concentration of substrate is increased?
A

the velocity plateau because Vmax is independent of the substrate concentration

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11
Q
  1. Can enzymes catalyze two or more substrates?
A

yes

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12
Q
  1. Is the pH different for different enzymes?
A

Blood 7.4
Stomach/gastric 1-2
Intestine tract 8-9
Saliva 7-9
Bile 7.7
Urine 5-8

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13
Q
  1. Which kinds of enzyme inhibitors exits?
A

Allosteric
Reversible
Proteolytic activation
Non/ competitive inhibitors

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14
Q
  1. What is competitive inhibition?
A

When the inhibitor binds to the catalytic site, no place for substrate

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15
Q
  1. What is non-competitive inhibition?
A

when the enzyme binds to a different site (allosteric site)

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16
Q
  1. What is an allosteric site?
A

any other region other than the catalytic site

17
Q
  1. What is the definition of an allosteric activator and inhibitor?
A

activator: enhancer of protein activity
inhibitor: decreases protein activity

18
Q
  1. What is a reversible covalent modification of an enzyme? Give an example.
A

no-blockage present, processes or de/-phosphorylating an enzyme
- phosphorylation
-methylation
-Adenylation

19
Q
  1. What is a proteolytic activation?
A

irreversible process where cleavage occurs to peptide bonds

20
Q
  1. What are zymogens?
A

an enzyme, protein or hormone synthesized into the inactive precursor
- fibrinogen
(-gen) or (Pro-)