Catalysis Considerations – Enzyme Classification by Kevin Ahern, PhD

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About the Lecture

The lecture Catalysis Considerations – Enzyme Classification by Kevin Ahern, PhD is from the course Enzymes and Enzyme Kinetics.


Included Quiz Questions

  1. R/T flipping occurs independently of the binding of substrate.
  2. The binding of the substrate causes the enzyme to flip the T/R state.
  3. The R-state is favored.
  4. The binding of allosteric effector(s) causes the enzyme to flip states.
  1. The binding of substrate molecules causes the enzyme to flip T/R states.
  2. The flipping occurs independently of the binding of the substrate.
  3. The R-state is favored.
  4. The binding of the product(s) causes the enzyme to flip states.
  1. Conformational changes in the enzyme by the binding of effector molecules.
  2. Amino acid sequence changes in the enzyme by the binding of effector molecules.
  3. Formation of new phosphodiester bonds in the enzyme by the binding of effector molecules.
  4. Formation of new peptide bonds in the enzyme by the binding of effector molecules.
  5. Peptide bond breakage in the enzyme by the binding of effector molecules.
  1. According to the concerted model, the binding of substrates favors the equilibrium towards the T state of the enzyme.
  2. According to the concerted model, an enzyme exists in two states: R-state and T-state.
  3. The concerted model and sequential model explain the allosteric regulation of enzymes.
  4. The sequential model states that binding of the substrate to the enzyme subunit facilitates the change of T form to R form.
  5. In the concerted model, the conformations of all the subunits change simultaneously.

Author of lecture Catalysis Considerations – Enzyme Classification

 Kevin Ahern, PhD

Kevin Ahern, PhD


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Clear, concise enough and interestingly explained
By Benjamin K. on 25. October 2017 for Catalysis Considerations – Enzyme Classification

It is very clearly and enthusiastically explained. You make Biochem easy to understand.