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22 notecards = 6 pages (4 cards per page)

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Biochem test 2

front 1

Name the enzyme classes

back 1

front 2

What is this reaction enzyme

back 2

oxioreductase

front 3

What is this reaction enzyme

back 3

transferase

front 4

What is this reaction enzyme

back 4

hydrolase

front 5

What is this reaction enzyme

back 5

Lyase

front 6

What is this reaction enzyme

back 6

Isomerase

front 7

What is this reaction enzyme

back 7

Ligase

front 8

What is a reaction intermediate

back 8

transient chemical species formed and decayed in reactions

front 9

Define rate limiting step

back 9

step with highest activation energy in a reaction

front 10

Explain effect of substrate concentration on enzyme activity

back 10

front 11

Explain effect of enzyme concentration on enzyme activity

back 11

front 12

Explain effect of temperature on enzyme activity

back 12

front 13

describe zero order kinetics

back 13

  • rate is constant and does not depend on the amount of substance
  • rate depends on presence of catalysts
  • Enzyme-catalyzed reactions exhibit zero-order kinetics when the reactant concentrations are so high that the enzyme is completely saturated with reactant molecules

front 14

describe first order kinetics

back 14

  • Rate is proportional with the amount of substrate present
  • Description of a reaction whose rate depends on the first power of the concentration of a single reactant

front 15

Graphs for 0,1st, and 2nd order reactions

back 15

front 16

Michaelis Menton Equation explaination

back 16

  • Has undergone modifications but is still the basic model for non-allosteric enzymes.
  • KM - Inverse measure of the affinity of the enzyme for the substrate; Lower the KM, the higher the affinity
  • Km=michaelis constant
  • Enzymes can only process so fast.
    • At low substrate → rate increases almost linearly
    • At high substrate → enzyme becomes saturated, rate levels off
    • v: reaction rate
  • [S]: substrate concentration
  • Vmax⁡: maximum rate (when enzyme is saturated)
  • Km​: Michaelis constant (substrate concentration at half Vmax⁡)

front 17

what is lineweaver burk graph

back 17

  • double reciprocal plot of enzyme kinetics

front 18

What are the equations for x intercept, y intercept, and slope on lineweaver burk graph

back 18

x int= -1/Km

y int =1/Vmax

slope=Km/Vmax

front 19

practice lineweaver burk calcs

back 19

front 20

reversible and irreversible inhibitors

back 20

front 21

what competitive inhibitors do in terms of enzymatic output and graph information

back 21

front 22

what non-competitive inhibitors do in terms of enzymatic output and graph information

back 22

  • Inhibitor does not interfere with substrate binding

–Value of Vmax decreases, and value of KM remains the same

  • Increasing substrate concentration cannot overcome noncompetitive inhibition

–Inhibitor and substrate are not competing for the same site