How do you overcome competitive inhibition?
Answer: By simply adding more substrate
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Bio Chemistry
- What is an international unit (IU) in enzyme kinetics?
- What is the slope in the Lineweaver-Burk plot?
- What does the turnover number mean in enzyme kinetics?
- What happens during uncompetitive inhibition?
- What happens during noncompetitive inhibition?
- What happens during competitive inhibition?
- What are the non-covalent modes of inhibition?
- Why is the Induced Fit Model deemed to be more correct than the Lock and Key Model?
- What are the two models of substrates binding to enzymes, and which is deemed to be more correct?
- What are the definitions of apoenzymes and holoenzymes and what is the difference between them?
- What are the definitions of apoproteins and holoproteins and what is the difference between them?
- True or false: All cofactors are coenzymes.
- Pertaining to enzymes, what is a cofactor?
- What does the fourth number indicate in the Enzyme Commission number for an enzyme?
- What does the third number mean in the Enzyme Commission number of an enzyme? (hint: it is directly related to the second number)
- What does the second number mean in the Enzyme Commission number of an enzyme?
- In the four-letter coding (Enzyme Commission number) of enzymes, what does the first digit signify?
- What are the six classes of enzymes, and what are their numbers according to the enzyme commission numbering system?
- How exactly do active sites catalyze reactions when a substrate is bound to it?
- How does X-Ray Crystallography separate proteins?
- How does mass spectrometry (electrospray ionization) separate proteins?
- How does electrophoresis separate proteins?
- How does gel-filtration separate proteins?
- How does ion-exchange chromatography separate proteins?