Chapter 6- The Behavior of Proteins: Enzymes Flashcards

1
Q

catalysis

A

the process of increasing the rate of chemical reactions

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2
Q

enzymes

A
  • biological catalysts, usually globular proteins with self-splicing RNA as the only exception
  • can increase the rate of a reaction by a factor of 10^20
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3
Q

standard free energy (changeG)

A

the difference between the energies of reactants and products under standards conditions

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4
Q

do enzymes alter the equilibrium constant of a reaction or free energy change?

A

nope

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5
Q

activation energy

A

the energy required to start a reaction

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6
Q

what type of reaction has a higher activation energy?

uncatalyzed or catalyzed

A

uncatalyzed (so the rate is slower)

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7
Q

sponanteous reactions have what type of delta g

A

negative

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8
Q

transition state

A

intermediate stage in a reaction where old bonds break and new bonds form

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9
Q

what happens to the rate of a chemical reaction when you increase temperature?

A

goes faster

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10
Q

isoenzymes

A

multiple forms of an enzyme that catalyze the same overall reaction but have subtle physical and kinetic parameters

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11
Q

rate constant

A

a proportionality constant in the equation that describes the rate of a reaction

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12
Q

exponents in the rate equation are determined…

A

experimentsally

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13
Q

first order

A

described a written whose rate depends on the first power of the concentration of a single reactant

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14
Q

second order

A

describes a reaction whose rate depends on the product of the concentrations of two reactants

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15
Q

zero order

A
  • refers to a reaction that proceeds at a constant rate, independent of the concentration of reactant
  • sometimes depends on catalysts
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16
Q

substrate

A

-reactant in an enzyme-catalyzed reaction

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17
Q

where does the substrate bind? and by what type of interactions?

A

enzyme; noncovalent

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18
Q

active site

A

part of enzyme where substrate binds and reactant takes place

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19
Q

why does substrate bind to enzyme

A

because of highly specific interactions between the substrate and the side chains and backbone groups of the amino acids making up the active site

20
Q

lock and key model

A

substrate and active site exactly match each other in shape

21
Q

induced fit model

A

binding of the substrate induces a conformational change in the enzyme that results in a complementary fit after substrate is bound

22
Q

MM rate constant Eqn Terms

A

k1: rate constant for formation of ES
k-1: rate constant for ES–> E + S
k2: rate constant for ES—> E + P

23
Q

rate depends on

A

substrate concentration

24
Q

Vmax

A

maximum velocity

25
Q

Km

A
  • substrate concentration at which the reaction performs at one half its vmax
  • inverse measure of the affinity of the enzyme for the substrate
  • equals the concentration of substrate at which 50% of the enzyme active sites are occupied by substrate
26
Q

lower Km=

A

higher affinity of enzyme for substrate

27
Q

steady state

A

formation of ES complex equals the rate of its breakdown

28
Q

michealis constant

A

Km; a numerical value for strength of binding of a substrate to an enzyme

29
Q

michealis-menten eqn formula

A

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

30
Q

When [S]=Km, then…

A

V= Vmax [S]
________
[S] + [S]

and

V= Vmax
______
2

31
Q

what type of curve describes the rate of a nonallosteric enzymatic reaction?

A

hyperbolic

32
Q

Lineweaver-Burk Double Reciporcal Plot

A
  • graphical method for analyzing the kinetics of enzyme-catalyzed reaction
  • x axis: 1/[S]= (nm)-1
  • y axis: 1/Vo= sec/nm
  • slope: Km/Vmax
33
Q

Keq=

A

[E][S]
_____
[ES]

34
Q

larger Km

A

less tightly enzyme bound to substrate

35
Q

turnover number (kcat)

A
  • number of moles of substrate that react per second per mole of enzyme
  • assumes enzyme is fully saturated with substrate and reaction is proceeding at max rate
36
Q

chymotrypsin

A
  • proteolytic enzyme that preferentially hydrolyzes amide bonds (peptide bonds) adjacent to aromatic amino acid residues
  • can cleave peptide bonds
  • catalyzes hydrolysis of ester bonds
  • hyperbolic
37
Q

ATCase

A
  • allosteric enzyme that catalyzes an early reaction in pyrimidine biosynthesis
  • signmodial
38
Q

ATCcase and hemoglobin are

A

allosteric proteins (myoglobin and chymotprsin aren’t)

39
Q

inhibitor

A

substance that decreases the rate of enzyme catalyzed reaction

40
Q

reversible inhibtor

A

can bind enzyme and then be released, leaving enzyme in original condition

41
Q

irreversible inhibitor

A

reacts with enzyme to produce protein that is not enzymatically active and from which the original enzyme can’t be regenerated

42
Q

compettive inhibitor

A
  • decreases enxyme activity caused by binding of substrate in active site
  • inhibitor competes with substrate for active site
  • SLOPE CHANGES
  • KM INCREASES
43
Q

how can competitive inhibition be overcame?

A

very high substrate concentration

44
Q

noncompetitive inhibitor

A
  • substrate binds to place other than the active site, but distorts active site so that reaction is inhibited
  • SLOPE CHANGES
  • VMAX DECREASES
45
Q

Uncomepetitive inhibitor

A
  • inhibitor can bind to ES, but no free E
  • lines are parallel
  • Vmax decreased
  • apparent Km decreased
46
Q

irrevisible inhibition

A

covalent binding of an inhibitor to an enzyme, causing permanent inactivation

47
Q

suicide substrates (trojan horse)

A

molecules used to bind to an enzyme irreversibly and inactivate it