Chapter 7 Flashcards

1
Q

enzymes

A

regulate chemistry of cells and organisms

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2
Q

catalysts

A

enhance rate of reactions

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3
Q

active site

A

region where substrate binds

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4
Q

lock and key model

A

unbound substrate is complementary in shape to the enzyme

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5
Q

induced fit

A

some enzymes assume a complementary shape after the substrate has initially bound

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6
Q

cofactor

A

small non-protein accessory molecule whose presence is required for enzyme activity

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7
Q

apoenzyme

A

without its cofactor

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8
Q

holoenzyme

A

cofactor-bound, active enzyme

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9
Q

prosthetic groups

A

cofactors that binds their enzyme tightly and rarely dissociate

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10
Q

Michaelis-Menten

A

V = Vmax[S] / [S] + Km

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11
Q

Turnover number (kcat)

A

kcat = Vmax / [Et]

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12
Q

specificity constant

A

kcat / Km

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13
Q

temperature

A

as temp increases, rate of reaction increases

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14
Q

pH

A

enzymes function of pH displays a bell-shaped curve

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15
Q

enzymatic activators

A

bind enzymes and increase their activity

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16
Q

enzymatic inhibitors

A

decrease an enzyme’s activity

17
Q

competitive inhibitor

A

-prevents the substrate from binding the active site of the enzyme
- Vmax stays the same but Km increases

18
Q

uncompetitive inhibitor

A

-binds only to the enzyme-substrate complex
- Vmax and Km are reduced

19
Q

mixed inhibitor

A

-bind to an enzyme molecule independently or simultaneously
-Km can increase or decrease while Vmax decreases

20
Q

noncompetitive inhibition

A

affects Vmax but not Km

21
Q

Lineweaver for inhibition

A
  • competitive (meet on y-axis)
  • uncompetitive (parallel)
  • mixed (meet off axis)
  • noncompetitive (meet on x-axis)
22
Q

irreversible inhibitors

A

permanently inactivate an enzyme

23
Q

kinetic mechanism

A

order of binding of substrates and release of products