CEN 551 Biochemical Engineering. Instructor: Dr. Christine Kelly. Review chapter 3, 4, 5 Section 4.6 - Regulation. Schedule. Today 1/27: chapter 3 and 4 review, chapter 5 Thursday 1/29: chapter 6 and 7 Tuesday 2/3: review for exam 1 Thursday 2/5: exam 1 (chapters 1-7).
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Instructor: Dr. Christine Kelly
Review chapter 3, 4, 5 Section 4.6 - Regulation
maximum reaction rate
Da>>1 diffusion limiting
Da<<1 reaction rate limiting
Sb = bulk substrate
kL = mass transfer coefficient
Write down vocabulary from chapter 3 that you think I expect you to know without looking in the text or notes.
Factors that can cause denaturation of enzymes
Rapid equilibrium assumption
Quasi-steady state assumption
Types of inhibition
How does temperature affect enzyme kinetics
What are immobilized enzyme
Advantage/disadvantage of immobilized enzyme
Process in converting reactants to products in immobilized systems
exon intron exon
intron degraded before translation
1. Genetic level (control of transcription). Controlling the amount of enzymes. Most common in procaryotes.
2. Enzymatic level (control of product formation). Controlling activities of enzymes. Most common in eucaryotes.
GENESGenetic Level Control
Activator binding site
If tryptophan low, the repressor does not bind tryptophan and thus cannot bind to operator. RNA polymerase can bind to the promoter.
If tryptophan high, the repressor binds tryptophan, binds to the operator, where it blocks the binding of RNA polymerase to the promoter.
allosteric inhibitor changes the conformation of the enzyme, distorting the active site and reducing the ability to catalyze the reaction.
The relative permeability of a synthetic lipid bilayer to different classes of molecules. The smaller the molecule and, more important, the fewer its favorable interactions with water (that is, the less polar it is), the more rapidly the molecule diffuses across the bilayer. Note that many of the molecules that the cell uses as nutrients are too large and polar to pass through a pure lipid bilayer.