Enzymes Flashcards

1
Q

Enzymes as biological catalysts

A
  1. Enzymes are proteins that increase the rate of reaction by lowering
    the energy of activation
  2. They catalyze nearly all the chemical reactions taking place in the
    cells of the body.
  3. Not altered or consumed during reaction.
  4. Reusable
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2
Q

When the Substrate (S) binds in an
Enzyme active site, an…

A

Enzyme-substrate complex is formed

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3
Q

Enzymes may recognise and catalyse:

A
  • single substrate
  • a group of similar substrates
  • particular type of bond
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4
Q

Enzymes increase reaction rates by…

A

Decreasing activation energy

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5
Q

What happens to ΔG when an enzyme is added

A

It remains unchanged

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6
Q

What affects enzyme activity

A

Three factors

  1. Environmental Conditions – pH, Temperature,
    Substrate concentration
  2. Cofactors and Coenzymes
  3. Enzyme Inhibitors
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7
Q

What is an apoenzyme and a holoenzyme

A

Apoenzyme -
An enzyme without its non-protein component (Cofactor) it is therefore inactive

Holoenzyme -
An enzyme with its non protein component (cofactor) it is therefore active

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8
Q

Cofactor vs coenzyme vs prosthetic group

A

Cofactor
-Non-protein compound, inorganic/organic
-Bound covalently or loosely to enzyme
-Required for catalysis: coenzymes, prosthetic groups, metal ions (Fe2+, Mg2+, Ca2+, Zn2+),

Coenzyme
-Non-protein component, organic
-Loosely bound to apoenzyme by non-covalent bond
-NAD, FAD, ATP, vitamins (contribute to catalysis)

Prosthetic group
-Permanent part of 3D structure
-Tightly bound to apoenzyme by covalent bonds
-Heme in hemoglobin, does not dissociate from enzyme until it is degraded

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9
Q

What is irreversible inhibition

A

Inhibitors covalently interact with enzyme that their inhibition is irreversible

Any compound that modifies the enzyme active site

Modified enzyme is dead and can only be overcome with new
enzymes

Neurotoxins are irreversible inhibitors as the inhibit acetylcholine esterase in the synapses of neurones

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10
Q

What is non competitive inhibition

A

Noncompetitive inhibitor binds to a site on enzyme other than the active site

Reduces enzyme activity but does not affect binding of substrate

Binds to Enzyme or
Enzyme-Substrate complex

Inhibition is reversible

Extent of inhibition depends on inhibitor concentration

Cyanide is an example of a non competitive inhibitor as it binds to cytochrome c oxidase enzyme in electron transport chain so ATP can no longer be made as enzyme can not pass electrons to oxygen so only anaerobic respiration is possible, the build up of lactic acid results in death

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11
Q

What is Uncompetitive inhibition

A

Inhibitor binds only to Enzyme-substrate complex

Inhibitor affects substrate binding by increasing enzymes affinity for substrate

The Enzyme-substrate-inhibitor complex is inactive and decrease rate of reaction

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12
Q

What is allosteric inhibition

A

Enzymes contain both an active site and a modulator site

Inhibitor binds to enzyme at modulator site, changes conformation of enzyme

Decrease catalytic activity
of the substrate at the active site

E.g. Direct Thrombin Inhibitors act as anticoagulants of Thrombin

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13
Q

What is feedback inhibition

A

Enzyme activity is inhibited by end product in a biochemical pathway.

Occurs when there is buildup of product being produced.

Negative feedback slows down the production to maintain homeostasis in a cell.

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14
Q

What is an apenzyme

A

Enzyme without cofactor

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15
Q

What is holoenzyme

A

Enzyme with cofactor

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16
Q

What is vmax

A

Full saturation so substrate conc no longer limiting factor