Reversible Enzyme Inhibition Flashcards

1
Q

In this type of inhibition, the inhibitor competes with the substrate for the active site of the enzyme

A

competitive

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2
Q

True or false? a competitive inhibitor usually has some structural similarity to the substrate

A

true

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3
Q

What does a competitive inhibitor bind to?

A

free enzyme

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4
Q

Competitive inhibition increases the “apparent” ___ of the enzyme

A

Km

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5
Q

The following describes what type of inhibition? By removing some of the free enzyme from the reaction, it appears to take a higher [S] to achieve 1/2 Vmax

A

competitive

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6
Q

What does competitive inhibition look like on lineweaver - burk plot?

A

X intercept is different but lines go through Y intercept at same point

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7
Q

In competitive inhibition, Vmax is unaffected. Explain why.

A

since by increasing [S], the inhibition can be overcome and Vmax can be achieved

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8
Q

___ are competitive inhibitors of the rate limiting enzyme of cholesterol biosynthesis

A

statins

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9
Q

The following version of the michaelis-menten equation describes what type of inhibition:

v = Vm[S] / Km(1+[I]/Ki)+[S]

A

competitive

note: only Vm[S] is on top

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10
Q

A noncompetitive inhibitor binds to either ___ or ___

A

E; ES

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11
Q

Do noncompetitive inhibitors bind to the active site?

A

no, therefore don’t compete with substrate binding

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12
Q

Since a noncompetitive inhibitor doesn’t compete with the S, increasing [S] will have what effect?

A

none, won’t overcome the inhibition

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13
Q

A noncompetitive inhibitor decreases the “apparent” ___ of the enzyme

A

Vmax

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14
Q

The effect of a ____ inhibitor is to effectively reduce the number of active enzyme molecules, which has the appearance of reducing [Etotal]

A

noncompetitive

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15
Q

What does noncompetitive inhibition look like on a lineweaver-burk plot?

A

X intercepts are the same but lines cross at different points on Y intercept

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16
Q

The following version of the michaelis-menten equation describes what type of inhibition:

v = Vm[S]/(1+[I]/Ki)//Km+[S]

A

noncompetitive

note: only Km + [S] on bottom

17
Q

Many heavy metals such as Hg and Pb interact with the -SH groups on enzymes and act via ____ inhibition

A

noncompetitive

18
Q

An uncompetitive inhibitor binds only to the ___ of an enzyme

A

ES

19
Q

In uncompetitive inhibition, it is proposed that substrate binding alters the enzyme structure such that…

A

the inhibitor may subsequently bind

20
Q

The inhibitor does not compete with the substrate for the active site in uncompetitive inhibition. True or false?

A

true

21
Q

In uncompetitive inhibition, as [S] increases, so does inhibition since ES is required for the inhibitor, there for Vmax is ____

A

decreased

22
Q

What does uncompetitive inhibition look like on a line-weaver burk plot?

A

parallel lines

23
Q

In the presence of an uncompetitive inhibitor, there will be an apparent Vmax ___ than the true Vmax and an apparent Km ___ than the true Km

A

less; less

24
Q

The following version of the michaelis-menten equation describes what type of inhibition:

v = Vm[S]/1+[I]/Ki//Km/1+[I}/Ki + [S}

A

uncompetitive

note: a whole lot going on up top and on bottom

25
Q

____ inhibitors are rare in single substrate enzymes but more common in multi-substrate enzymes

A

uncompetitive