Topic 3-L3 - Enzymes Flashcards

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1
Q

(generally) Proteins made by cells that act as

A

catalysts

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2
Q

There are RNA enzymes as well, called

A

ribozymes

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3
Q

Vast majority of enzymes are

A

proteins – metabolism mediated by

protein enzymes

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4
Q

Are catalysts specific to specific rxns?

A

Yes

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5
Q

Enzyme names generally end with the “___” suffix.

A

ase

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6
Q

Formation of H2O is exergonic and energetic s are favourable, but won’t occur without catalyst why?

A

Activation energy way to high and needs to be lowered

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7
Q

Enzymes work by lowering the

A

activation energy of a reaction, therefore increasing the rate for rxn

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8
Q

Do catalysts change energetics of ΔG or equilibrium of rxn

A

They do NOT change the energetics (ΔG) or the equilibrium of the reaction

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9
Q

How do enzymes lower the activation energy of a reaction??

A
  • Local concentrations of substrates are increased at the active site of the enzyme
  • enzymes alter the electronic distribution and
    conformational structure of the substrate(s), which enhances reactivity.
  • stabilization of transition metals
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10
Q

Catalysts stabilizing transition metals involve

A

the use of coenzymes or prosthetic

groups – some use metallic elements (E.g. - Fe, Mg, Zn, Co…)

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11
Q

Steps for a enzyme-catalyze rxn

A

1) substrate bound to enzyme active site
2) enzyme substrate complex forms
3) strain is placed on bond
4) produces are released
5) enzyme is ready to begin new catalytic cycle

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12
Q

How do enzymes influence cell metabolism?

A

Enzymes catalyze specific reactions, allowing the for accumulation of those specific products

  • In metabolic pathways, products from one reaction are the reactants in the next – prevents accumulation of products of the individual reactions (accumulation of products promotes the reverse reaction)
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13
Q

Most biological reactions will not occur at a significant rate in the absence of an enzyme ?

A

Yes

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14
Q

Enzyme activities can be controlled by regulating the amounts of the

A

enzymes or by controlling their activity (via competetive inhibitors)

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15
Q

Competitive inhibitors of an

A

enzyme “fit” in the same active sit as

the substrates – inhibit substrate binding (and thus the reaction)

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16
Q

Competetive inhibitors is the way many drugs work (example below is from

A

sulfa drugs – antibiotics that inhibit folate biosynthesis)

17
Q

Positive effector (“allosteric activator”):

A

Promotes binding of substrate and catalysis

18
Q

Negative effector (“allosteric inhibitor”):

A

Prevents substrate from binding

19
Q

Types of effectors

A

postive (allosteric activator) and negative (allosteric inhibitor)

20
Q

Allosteric activators steps for action

A
  1. Effector binds to allosteric site
  2. Causes conformational change in active site
  3. Substrate fits into active site
  4. Substrate will be converted to product
21
Q

Allosteric inhibitors steps for action

A

1) Effector binds at regulatory site
2) Causes conformational change in active site
3) Substrate can not bind (no “fit” in active site)
4) Reaction inhibited

22
Q

Absences of effector causes

A
  • Substrate binds to active site

- Catalysis proceeds

23
Q

Feedback inhibition is A common strategy used to

A

control metabolic pathways

24
Q

Feedback inhibition:

A
  • End product is negative modulator:
  • Binds to first enzyme in pathway & inhibits its activity.
  • End product shuts down its own production when it’s in excess
  • Once end product used up, pathway resumes