Enzymes Flashcards

(18 cards)

1
Q

What are apoenzymes

A

They are enzymes with out a prosthetic group

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2
Q

What are haloenzymes

A

They are enzymes with a prosthetic group

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3
Q

What are the two general ways to increase the speed of chemical reactions

A
  1. Add heat
  2. Add a catalyst
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4
Q

True of false: Biological catalysts have different structure than other proteins

A

False, biological catalysts have the same structures as proteins

It is also stabilized by the same non-covalent interactions
- hydrophobic interactions
- hydrogen bonds
- ion pairs
- van der waals
- disulfide bridges depending on the environment

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5
Q

Are enzymes specific?

A

Yes enzymes are highly specific

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6
Q

Why do non-biological enzymes have a greater capacity for regulation

A

Because conformational change in protein structure is possible

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7
Q

How do enzymes work

A

Enzymes speed up reaction rates

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8
Q

What is considered to be a high energy bond

A

It has to release a minimum of -25 kj/mol

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9
Q

How much energy does breaking a phophoanhydride bond create

A

-30 kJ/mol

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10
Q

Which chemical reactions are thermodynamically favorable (exergonic or endergonic)

A

Exergonic because they have a negative change in G
(They are spontaneous)

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11
Q

What is the highest free energy state in a reaction, what does it do?

A

The transition state
It determines the activation barrier for the reaction
Thermodynamics

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12
Q

What determines the speed of a biochemical reactions

A

The size of the activation energy barrier
Enzymes can also speed up reactions
(Kinetics)

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13
Q

What are 4 ways that catalysts lower the activation energy barrier

A
  1. Remove substrates from aqueous solutions (desolvation)
  2. Proximity and orientation effects
  3. Taking part in the reaction mechanism
  4. Stabilizing the transition state
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14
Q

What are the 2 different sites that an active site can be made of

A
  • catalytic site
  • substrate binding site
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15
Q

What is the correct model for enzyme and substrate binding, describe it

A

Induced fit model

Shape of active site resembles TS
It removes substrates from aqueous solution (basically isolates the substrate) and squeezes out H20

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16
Q

What are the advantages of an enzyme isolating the substrate

A
  1. Prevents water interference
  2. Forms H bonds is more effective in a non (Aq) env
  3. It eliminates energy barrier that the solvent makes
17
Q

What do co-factors do to enzymes

A

Help with their function

18
Q

What amino acids can be involved in nucleophilic (covalent) catalysis?

A

Asp, Glu, Ser, Tyr, Cys, Lys, His