cofactors and coenzymes Flashcards

1
Q

define coenzyme

A

organic cofactor not permanently attached to the protein

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2
Q

define cofactor

A

non-protein component necessary for effective functioning of an enzyme (ions or organic molecules)

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3
Q

describe the similarities between cofactors, coenzymes and prosthetic groups.

A
  • coenzymes and prosthetic groups are both cofactors
  • cofactors and prosthetic groups can be organic or inorganic
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4
Q

describe differences between cofactors, coenzymes and prosthetic groups.

A
  • coenzymes are organic cofactors - not permanently attached to the protein
  • prosthetic groups are cofactors that are permanently attached to the enzyme
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5
Q

why is the chloride ion necessary for the correct formation of the amylase active site is a cofactor, not a coenzyme or prosthetic group

A
  • it is organic (coenzymes are organic)
  • it is not permanently attached (prosthetic groups are)
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6
Q

explain why zinc ions that form an important part of the structure of carbonic anhydrase is a prosthetic group, not a cofactor or coenzyme.

A
  • it is permanently attached (stating cofactor is ambiguous as they are both)
  • inorganic (coenzymes are organic only)
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7
Q

give two examples of coenzymes synthesised from vitamins in our diet.

A
  • NAD (vitamin B3)
  • NADP (vitamin B3)
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8
Q

define inorganic precursor enzyme

A

enzyme that requires biochemical change for it to become active

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9
Q

explain why inactive precursor enzymes may be produced

A
  • to prevent enzymes from causing damage within the cells producing them when released
  • when enzymes action needs to be controlled
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10
Q

describe 3 ways in which inactive precursor may be activated.

A
  • adding a cofactor
  • action of another enzyme
  • change in conditions
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11
Q

define apoenzyme

A

protein that forms an active enzyme by combination with a cofactor

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12
Q

define holoenzyme

A

active form of an enzyme

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13
Q

define zymogens

A

inactive enzymes that require a biochemical change (change in conditions/acted on by another enzyme) to become an active enzyme.

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14
Q

define proenzymes

A

inactive enzymes that require a biochemical change (change in conditions/acted on by another enzyme) to become an active enzyme.

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15
Q

give 2 examples of inactive precursor enzymes and describe how they are activated

A
  • pepsinogen: becomes pepsin when exposed to stomach acid (low pH)
  • trypsinogen: becomes trypsin when cleaved into active form by enteropeptidase
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