Enzymes I+II- Lecture 8/31/21 Flashcards

(42 cards)

1
Q

Elastase

A

A protease that destroys elastin, which destroys the lining of the lungs

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2
Q

How can enzyme activity be deficient

A

Enzyme isn’t made
Enzyme is made but has a mutation that lowers activity
Insufficient substrate
inhibited

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3
Q

Catalyst

A

Third party that alters the kinetics of a reaction without being altered itself

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4
Q

Oxidoreductases

A

Catalyze an oxidation-reduction rxn, ex: NAD+->NADH

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5
Q

Transeferases

A

Transfer of a chemical group ex: kinases

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6
Q

Hydrolases

A

Lysis of water, ex: protease

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7
Q

Lyases

A

A cleavage rxn not using water

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8
Q

Isomerases

A

Change of a molecular configuration

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9
Q

Ligases

A

Joining of two compounds ex: DNA poly

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10
Q

Delta G

A

Change in free energy

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11
Q

Spontaneous rxn

A

Has a negative delta G

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12
Q

Gibbs free energy equations

A

DeltaG=DH-TDS

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13
Q

Standard conditions for DGo

A

Certain temp, 1 M conc, except [H+] is pH of 7

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14
Q

Gibbs free energy in not standard conditions

A

DG=DGo+RTlnQ

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15
Q

Q

A

Q= [Products]/[reactants]

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16
Q

Equilibrium

A

When DG=0

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17
Q

Keq

A

Q at equilibrium

Keq=e>-DGo/RT

18
Q

When Q>Keq

A

The reaction goes in reverse

19
Q

When Q

A

Reaction proceeds forward, removal of product drives reaction forward

20
Q

Transition state

A

High energy intermediate, stabilization by catalyst allows for the activation energy to be lowered and the rxn to proceed faster

21
Q

Catabolism

A

The breakdown of energy yielding nutrients to gain energy in the form of ATP, NADH

22
Q

Anabolism

A

Using simple precursor molecules to build complex molecules needed for life, includes active transport and mechanical work

23
Q

Multibinding enzymes

A

Enzymes can bind more than one substrate, and often couple an exergonic rxn with an endergonic one

24
Q

Serine proteases

A

Proteolytic enzymes that catalyze peptide bond hydrolysis by using activated serine resides to add water and break the bond

25
Active site
Usually a crevice on the surface of the enzyme where the substrate binds
26
Velocity of an enzyme
The amount of product formed per unit time
27
Vmax
The point at which adding more substrate does not lead to an increase in reaction velocity (adding more enzyme increases Vmax)
28
Equation for velocity
V=Vmax[S]/(Km+[S])
29
Km
The concentration of substrate when v=1/2Vmax
30
What does Km tell us about enzyme affinity?
The lower the Km, the higher the affinity
31
Kcat
A measure of enzymatic efficiency, Kcat=Vmax/the enzyme concentration, “turn over” number. Characteristic of an enzyme
32
Lineweaver Burke plot
Linear derivation of MM plot, 1/v=(Km/Vmax)1/[S]+1/Vmax
33
Vmax on LB plot
The Y intercept is 1/Vmax
34
Km on LB plot
X intercept, -1/km
35
Competitive inhibitor
Binds in the active site, increases Km but does not effect Vmax
36
Non-competitive inhibitors
Binds to an allosteric site, Km is unaffective, Vmax is decreased
37
Zymogens
The active site is not formed correctly until cleavage event
38
A1-antitrypsin
Inhibits the elastase in the lungs, prevents lung degradation
39
Protein phosphorylation
Enzymes can be phosphorylated to change the shape and therefore function
40
Allosteric enzymes
Have t and r state, more sensitive to enzyme concentration
41
Feedback loops
Final product can inhibit the first enzyme in a pathway
42
Direct product inhibition
Inhibition of an enzyme by the direct product of that rxn.