Enzymes Flashcards

(50 cards)

1
Q

Enzyme defintion

A

Substance that increases rate of reaction but stays same as it was b4

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2
Q

Enzyme binds ______ to substrate

A

Reversibly

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3
Q

Enzyme substrate complex ______forms _______

A

Irreversibly
Product
Regenerates catalyst

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4
Q

Active sites contain

A

Catalytic residues

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5
Q

Specifiticty of enzymes involve what forces

A

Van der Waals
Electrostatic
H-bonding
Hydrophobic interactions

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6
Q

Enzyme mechanismm

A

Facilitates formation of transition state

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7
Q

Cofactors

A

Small molecules bound to enzyme

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8
Q

Enzyme with/without cofactor

A

Without - apoenzyme (inactive)

With - holoenzyme (active)

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9
Q

Two groups of cofactors

A

Metal ions and small organic molecules

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10
Q

Coenzymes

A

Small organic cofactors

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11
Q

Prosthetic groups

A

Coenzymes tightly bound

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12
Q

_____ are often precursors to coenzymes

A

Vitamins

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13
Q

V

A

Number of moles formed per second

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14
Q

Km

A

Concentration of S that is 1/2 of Vmax

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15
Q

Km measures

A

How tightly substrate binds

Lower Km = more tightly bound = more likely to form product

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16
Q

V relationship to Vmax and Km

A

Proportional to Vmax

Inversely proportionalto Km

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17
Q

Line-weaver Burke improtant points

A
X-intercept = 1/-Km
Y-intercept = 1/Vmax
Slope = Km/Vmax
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18
Q

Reversible inhibition types

A

Competitive and noncompetitive

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19
Q

Competitve inhibiton

A

Binds active site
Overcome with more substrate
Changes Km

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20
Q

Noncompetitive inhibition

A

Binds other site
Cannot be overcome with substrate
Changes Vmax

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21
Q

Irreversible inhibtion typically

A

Involves covalently bound

Can bind anywhere

22
Q

Kinase

A

Transfer of phosphate using ATP

23
Q

Phoshorylase

A

Adds inorganic phosphate to substrate iwhtout ATP

24
Q

Phosphatase

A

Removes phosphatre

25
Dehydrogenase
Redox
26
Hydroxylase
Add hydroxyl
27
Carboxylase
Transfers CO2
28
Mutase
Relocates functional group within a molecule
29
Feedbakc inhibition
Product regulates earlier enzyme | Common in metabolism
30
Allosteric and how is it different than noncompetitive
Has allosteric sites that can be activated or inhibited | Sigmoidal M-M kinetics
31
Isozymes and example
Differ in sequence but catalyze same reaction Allows fine-tuning Lactate dehydrogenase
32
H form and M form of lactate dehydrogenase
H - Heart (higher affinity) | M - skeletal (lower)
33
Covalent modification (which are reversible and which are not?)
Reversible - phosphorylation, acetylation | Irreversible - attachment of lipid group that localizes protein to a membrane
34
Autoinhibition and example
Portion of enzyme keeps it inactive by regulatory subunits until activator binds Protein Kinase A
35
Mechnaism of autoinhibition
Regulatory has pseudosubstrate sequence that binds active site of catalytic units...activator binds to regulatory sequence
36
Zymogens
Inactive precursors | Most undergo proteolytic cleavage to become active
37
Types of zymogens
Digestive enzymes Blood clotting Collagenase Capsases
38
Aspirin common name and goup
Acetylsalicylic acid | NSAID
39
NSAID mechanism
Inhibit COX (cyclooxygenase enzymes)
40
Isoforms of COX
COX 1 and COX 2 (means it is an isoenzyme)
41
Aspirin targets which forms of COX?
Bot h
42
COX enzyme reaction
Turn arachidonic acid into PGG2...eventually forms prostaglandins and thromboxane
43
Prostaglandins
Make neurons more sensitive Dilate or constrict vessels Prevent or promotoe platelet aggregation
44
Aspirin...reversible or irreversible?
Irreversible...adds acetyl group
45
Aspirin reaction with Cox 1 and COx 2
Ser530 COX 1 | Ser 516 Cox 2
46
Other NSAIDs bind to COX enzymes
Competitively and reversibly
47
Statins
Competitive inhibitors of HMG-CoA reductase | Reduce cholesterol synthesis
48
HMG-CoA reductase reaction and what it requires
HMG-CoA to mevalonic acid | 2 NADPH
49
HMG-CoA reductase location and catalytic domain
Membrane protein | Cat. domain - cytosol
50
Statin mechanism
Binds to active site of HMG-CoA reductase and excludes HMG-CoA