Biochem L5R Flashcards

1
Q

What is the Michaelis-Menten, what are the values associated with the equation?

A

1.VELOCITY expressed as the rate of substrate to product conversion per min. & velocity depends on concentration of [s].

  1. Michaelis-Menten equaiton explains change in velocity related to substrate concentration.

km=affinity of enzme to a particular substrate.

small Km= High affinity

large Km= low affinity

Vmax= Maximal reaction velociyt

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2
Q

Differentiate between Lineweaver and Burk Equation.

A
  1. Lineweaver-Burk equation ( double reciprocal plot.)
    - Required less points to make a plot
    - Make the extapolation easier.
  2. Liner slope
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3
Q

what do Glucokinase and hexokinase do? explain the chart.

A

1.Isozymes catalyze 1st step in glucose metabolism.

Ex. Hexokinase I allows RBCs to use glucose when plasma level is low.

Ex. Glucokinase found in liver & pancreatic beta cells

Promotes storage of glucose or insulin secretion.

Need help explaining the chart and what it means:

Glucose phoshorylation in liver…

1.increases and glucose level increase

2.Down as blood glucose levels fall

3.High Km of glucokinase prometes glucose storage

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4
Q

What are the major differences between Noncompetitive and Competitive inhibition? what is the following graph.

A
  1. Inhibitor, substance that can decrease the velocity of reaction.
    - Reversible inhibitor: binds to enzyme through noncovalent bonds, enzyme can funtion porperly by dilution or uping [s]
    - Irreversible Inhibition: Enzyme does not regain activity upon dilution. usually by covalent interacton of Inhibitor and Enzyme
  2. two kinds

1.Competitive : Inh. binds to same site of substrate,

  • Reversible by uping [s]
  • Vmax doesnt change
  • Km increased, more [s] needed to acheive 1/2 Vmax
    2. Noncompetitive: Inh. and substrate bind at different sites on the enzyme.
  • Inhibitor can bind to free enzyme or ES complex.
  • Irrevirsible
  • lower Vmax
  • Km stays the same ( no interference with substrate binding to enzyme.)
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5
Q

what are the different types of processes, to regulate enzymes activity by conformational changes?

A
  1. We can regulate enzymes activity by conformational changes.
  2. Allosteric activation or inhbition:
  3. Phosphorylation or other posttranslational modifications
  4. Protein-protein interaction
  5. proteolytic cleavage
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6
Q
A
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