Biochem L5R Flashcards
What is the Michaelis-Menten, what are the values associated with the equation?
1.VELOCITY expressed as the rate of substrate to product conversion per min. & velocity depends on concentration of [s].
- 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
Differentiate between Lineweaver and Burk Equation.
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Lineweaver-Burk equation ( double reciprocal plot.)
- Required less points to make a plot
- Make the extapolation easier. - Liner slope
what do Glucokinase and hexokinase do? explain the chart.
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
What are the major differences between Noncompetitive and Competitive inhibition? what is the following graph.
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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 - two kinds
1.Competitive : Inh. binds to same site of substrate,
- Reversible by uping [s]
- Vmax doesnt change
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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.)
what are the different types of processes, to regulate enzymes activity by conformational changes?
- We can regulate enzymes activity by conformational changes.
- Allosteric activation or inhbition:
- Phosphorylation or other posttranslational modifications
- Protein-protein interaction
- proteolytic cleavage