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

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
Q

Active site

A

Usually a crevice on the surface of the enzyme where the substrate binds

26
Q

Velocity of an enzyme

A

The amount of product formed per unit time

27
Q

Vmax

A

The point at which adding more substrate does not lead to an increase in reaction velocity (adding more enzyme increases Vmax)

28
Q

Equation for velocity

A

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

29
Q

Km

A

The concentration of substrate when v=1/2Vmax

30
Q

What does Km tell us about enzyme affinity?

A

The lower the Km, the higher the affinity

31
Q

Kcat

A

A measure of enzymatic efficiency, Kcat=Vmax/the enzyme concentration, “turn over” number. Characteristic of an enzyme

32
Q

Lineweaver Burke plot

A

Linear derivation of MM plot, 1/v=(Km/Vmax)1/[S]+1/Vmax

33
Q

Vmax on LB plot

A

The Y intercept is 1/Vmax

34
Q

Km on LB plot

A

X intercept, -1/km

35
Q

Competitive inhibitor

A

Binds in the active site, increases Km but does not effect Vmax

36
Q

Non-competitive inhibitors

A

Binds to an allosteric site, Km is unaffective, Vmax is decreased

37
Q

Zymogens

A

The active site is not formed correctly until cleavage event

38
Q

A1-antitrypsin

A

Inhibits the elastase in the lungs, prevents lung degradation

39
Q

Protein phosphorylation

A

Enzymes can be phosphorylated to change the shape and therefore function

40
Q

Allosteric enzymes

A

Have t and r state, more sensitive to enzyme concentration

41
Q

Feedback loops

A

Final product can inhibit the first enzyme in a pathway

42
Q

Direct product inhibition

A

Inhibition of an enzyme by the direct product of that rxn.