Day 10 Flashcards

1
Q

enzymes are complimentary to what

A

transition state

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2
Q

rate eon for a one substrate enzyme catalyzed reaction

A

micaelis menten eqn

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3
Q

what is Michaelis menten eqn

A

initial velocity = (vmax x [S])/km + [S]

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4
Q

for reactions with two steps, km equals what

A

km= (k2+k-1)/k1

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5
Q

what represents slope in line weaver burk

A

Km/vmax

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6
Q

what represents y int in line weaver burk

A

1/vmax

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7
Q

enzyme inhibition has two broad categories, what are they

A

reversible and irreversible

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8
Q

competes with the substrate for the active site of an enzyme

A

competitive inhibotr

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9
Q

increases km, vmax uneffected

A

competitive inhibotor

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10
Q

WHAT is value of alpha prime for competitive inhibitor

A

1

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11
Q

slope changes, y int stays the same

A

competitive inhibition

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12
Q

binds at a site distinct from the substrate active site

A

uncompetitive inhibitor

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13
Q

binds only to the ES complex

A

uncompetitive inhibitor

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14
Q

causes decrease in both km and vmax

A

uncompetitive inhibiton

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15
Q

alpha value for uncompetitive inhibiton

A

1

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16
Q

y int changes, slope stays the same

A

uncompetitive inhibition

17
Q

binds at site distinct from the substrate active site

A

mixed inhibitor

18
Q

binds to either E or the ES complex

A

mixed inhibitor

19
Q

what does mixed inhibitor do to km and vmax

A

increases km, decreases vamx

20
Q

bind covalently with or destroy a functional group on an enzyme that is essential for the enzymes activity or form a highly stable non covalent association

A

irreversible inhibitor

21
Q

types of regulation of enzymes

A

positive or negative

22
Q

activators cause the curve to become what

A

more hyperbolic, more to the left

23
Q

inhibitor may cause the curve to become what

A

more sigmoidal, moving to right

24
Q

inactive precursor that is cleaved to form an active protease enzyme

A

zymogen

25
Q

precursors that are cleaved to form other proteins

A

pro protein or proenzyme