Enzymes Flashcards

1
Q

what is an enzymes tertiary structure?

A

globular proteins

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2
Q

what are scaffolding proteins?

A

the site of multiple enzymes working together to complete the same task

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3
Q

is the active site a small or large section of an enzyme?

A

a small portion

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4
Q

what is the equation of the active site?

A

binding site + catalytic site = active site

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5
Q

what is the activation energy?

A

the initial investment of energy to being the reaction and form the unstable intermediate

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6
Q

what is the transition state?

A

the unstable intermediate

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7
Q

how can the transition state occur?

A

adding heat

catalysts

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8
Q

what does the activation energy do to the viability of the reaction?

A

it makes the production of the final product energetically favorable

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9
Q

what happens to the activation of the reaction when an enzyme is used?

A

the activation energy is much lower

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10
Q

can enzymes change an endergonic reaction to an exergonic reaction?

A

no

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11
Q

are enzymes specific to reactions?

A

yes

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12
Q

how can enzymes lower the activation energy?

A

re-orientating substrates to increase efficiency allowing them to react
distorting substrate bonds allowing them to move to the transition state
adjusting the micro-environment of the substrates to allow substrates to interact and form product bonds.

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13
Q

what are cofactors?

A

non-protein chemicals that can aid biological reactinos

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14
Q

what are examples of inorganic cofactors?

A

pH, temperature and phosphorylation

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15
Q

what are examples of organic cofactors?

A

co-enzymes, often essential nutrients and minerals

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16
Q

what are cosubstrates?

A

transient cofactors

17
Q

what is the equation for inactive + cofactor = whole active enzyme

A

apoenzyme+cofactor=whole active enzyme

18
Q

what is a competitive inhibitor?

A

something that binds to the active site blocking the substrate

19
Q

what is an example of a competitive inhibitor?

A

penicilin

20
Q

what is a non-competitive inhibitor?

A

something that changes the shape of the binding site allowing the enzyme to react with different substrates

21
Q

what is an example of a non-competitive inhibitor?

A

lead - where the inhibitor fully reduces the rate of reaction the enzyme is capable of

22
Q

which can be out-competed - competitive or non-competitive inhibitors?

A

competitive inhibitors can be out-competed by increasing substrate concentration. this isn’t always possible with non-competitive inhibitors

23
Q

what is an example of an irreversible inhibitor?

A

toxins and poisons e.g. CO

24
Q

what are reversible inhibitors?

A

allosteric - usually w/ enzymes with multiple active sites and different substrates.

25
Q

what is an example of allosteric inhibitors?

A

co-operative binding e.g. O2 and haemoglobin