enzymes as catalysts Flashcards

1
Q

what do enzymes do

A
  • catalyse many chemical reactions which make up the process of metabolism
  • speeds up the rate at which a reaction reaches equilibrium
  • don’t affect the equilibrium position of a reaction
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2
Q

what are enzymes

A
  • Mostly proteins. except some types of RNA that are catalysts
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3
Q

what conditions do enzymes work in

A

Work at body temp in aqueous solutions and near neutral pH.

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4
Q

how much can enzymes increase rate

A

by a factor up to 10^20

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5
Q

how are enzymes specific

A

each enzyme has a limited range of substrates, some can distinguish stereoisomers

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6
Q

how are enzymes potent

A

each enzyme molecule can convert many substrate molecules into product per second

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7
Q

how to enzymes lower activation energy

A

Enzymes specifically bind and stabilise the transition state
The transition state is the reaction intermediate species which has the greatest free energy
Enzymes reduce the activation energy by providing alternative reaction pathways

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8
Q

what does the catalytic activity of enzymes rely on

A

presence of cofactors and coenzymes

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9
Q

what are cofactors

A

metal ions. forms a metal co-ordination centre in the enzyme. The enzyme may be referred to as a “metalloprotein”.

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10
Q

what are coenzymes

A

organic molecules. mostly associate with the enzyme only transiently. They change charge or structure during the reaction but are regenerated.

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11
Q

what are tightly bound coenzymes called

A

prosthetic group

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12
Q

what is an enzyme without a cofactor called

A

apoenzyme

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13
Q

what is an enzyme with a cofactor called

A

holoenzyme

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14
Q

what do vitamins have to do with enzymes

A
  • Most vitamins function as coenzymes, symptoms of vitamin deficiencies reflect the loss of specific enzyme activities. May be dietary or functional.
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15
Q

substrate binding to enzyme

A
  • Substrate binds to an active site: a cleft or crevice, contains amino acids essential for catalytic activity, contains amino acids for highly specific interactions
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16
Q

what is a lock and key model

A

Active site of unbound enzyme is complementary to the shape of the substrate

17
Q

what is an induced fit

A

Binding of substrate induces a conformational change in enzyme, results in complementary fit

18
Q

what can effect the performance of enzymes

A

temperature and pH. wrong conditions can denature the enzyme

19
Q

what are isozymes

A

they are isoforms of enzymes.

20
Q

what do isozymes do

A

they catalyse the same reaction but have different properties and structure (and sequence)

21
Q

where are isozymes synthesised

A
  • synthesised during different stages of foetal and embryonic development
22
Q

where are isozymes present

A

different tissues, different cellular locations

23
Q

what can be measured in tissue that can help diagnose

A

isozymes

24
Q

what type of isozyme is produced in the skeletal muscle

A

M form

25
Q

where is B for isozyme formed

A

in the brain

26
Q

what organ produces M and B type isozyme

A

heart

27
Q

how do isozymes help suggest a stroke/tumour has occured

A

when B type isozymes from the brain are present in blood

28
Q

what does appearance of heart type isozymes in blood suggest

A

heart attack