Enzymes Flashcards

1
Q

what do enzymes do?

A

speed up the rate at which a reaction reaches equilibrium

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2
Q

what do enzymes bind to and what do they do to this molecule?

A

the transition state

they stabilize it

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3
Q

what is the transition state?

A

the reaction intermediate species with the greatest free energy

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4
Q

what do enzymes reduce and how?

A

the activation energy

by providing alternative reaction pathways

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5
Q

what is glycogen storage disease?

A

an enzyme deficiency that results in the failure of glycogen to enter its transition state

this results in defective synthesis and breakdown of glycogen

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6
Q

how many types of glycogen storage diseases are there and why?

A

11

due to defects in 12 glycogen/glucose metabolising enzymes

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7
Q

what is the most common glycogen storage disease and describe its symptoms?

A

von gierke’s disease

hypoglycaemia, ulcers, hepatomegaly, bowel inflammation

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8
Q

how are glycogen storage diseases treated?

A

slow release glucose meals

feed little and often to mimic glycogen conversion to glucose

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9
Q

what are cofactors?

A

inorganic metal ions that may be needed for enzyme function

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10
Q

what are coenzynes?

A

organic molecules that may be needed for enzyme function

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11
Q

what are tightly bound coenzymes called?

A

prosthetic groups

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12
Q

what is an enzyme without a cofactor called?

A

an apoenzyme

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13
Q

what is an enzyme with a cofactor called?

A

a holoenzyme

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14
Q

what do active sites contain that enzymes require?

A

amino acids for catalytic activity and for specific interactions

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15
Q

where does a substrate bind to an enzyme?

A

the active site

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16
Q

what two models are used to describe how an enzyme binds to a substrat?

A

lock and key

induced fit

17
Q

describe the lock and key model

A

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

18
Q

describe the induced fit model

A

binding of the substrate induces a conformational change in the enzyme, resulting in a complimentary fit

19
Q

what are isozymes?

A

isoforms of enzymes

catalyse the same reaction but have different structure and properties

20
Q

name a protein thats isozymes can be used for diagnostic purposes

A

creatinine kinase

21
Q

what are the two isoforms of CK and where are they made?

A

M form in skeletal muscle (MM)

B form in the brain (BB)

22
Q

what type of CK is made by the heart?

A

both, forms a heterodimer (MB)

23
Q

what does appearance of BB CK in the blood suggest?

A

a stroke or brain tumour

24
Q

what does the appearance of MB CK In the blood suggest?

25
what carries out phosphorylation?
protein kinases
26
what are zymogens?
inactive enzyme precursors
27
how are zymogens activated?
cleavage of a covalent bond
28
what is Vmax?
the maximum velocity of a reaction
29
what is Km?
the concentration of a substrate which gives half Vmax
30
where is Vmax found when plotted on a straight line graph?
the Y intersection
31
where is Km found when plotted on a straight line graph?
the x intersection
32
what does a low Km suggest?
enzyme needs a little substrate to work at a half maximal velocity
33
what does a high Km suggest?
enzyme needs a lot of substrate to work at half-maximal velocity
34
what are the two classes of inhibition?
reversible | irreversible