Enzyme control Flashcards

1
Q

What does ALT presence in the blood indicate

A

liver damage

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2
Q

what converts fibrinogen to fibrin

A

thrombin

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3
Q

How does prothrombin associate with the plasma membrane

A

Its 2 modified gamma carboxy glutamate binds Ca2+

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4
Q

What carboxylates prothrombin’s glutamate residues

A

vitamin k

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5
Q

What vitamin K analog negates its effects

A

warfarin, thins blood

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6
Q

What class of enzyme is thrombin

A

serine protease (hyper catalytic Ser 195)

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7
Q

What does phosphorylation do to individual AA residues in enzymes

A

changes their charges

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8
Q

What conformational change occurs in the cleavage of prethrombin to thrombin

A

isoleucine moves to the catalytic spot

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9
Q

what kind of bond does antithrombin exhibit when it binds thrombin

A

covalent (common in zymogens)

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10
Q

what is the overall result of antithrombin binding

A

decreased blood coagulation

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11
Q

what does heparin do

A

increases antithrombin’s affinity for thrombin

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12
Q

Where is alpha-1 antitrypsin expressed and what is its function

A

It inhibits elastase activity in the lung

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13
Q

how does smoking damage the lungs

A

It oxidizes alpha-1 antitrypsin so that it no longer binds elastase

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14
Q

which AAs may be phosphorylated

A

Serine, threonine, and tyrosine (reversible process)

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15
Q

What are 2 rapid ways of activating enymes

A

zymogen cleaving and phosphorylation

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16
Q

what is the effect of competitive inhibitors on Vmax and Km

A

Vmax remains the same while Km increases

17
Q

what is the effect of noncompetitive inhibitors on Vmax and Km

A

Vmax decreases but Km is unaffected

18
Q

irreversible inhibitors affect what class of enzymes

A

serine proteases

19
Q

Where are allosteric effectors typically found and why

A

beginning of pathways to facilitate feedback inhibition

20
Q

Allosteric effectors tend to display what kind of binding

A

cooperative

21
Q

What forms do allosteric effectors exist in

A

taut and relaxed