Bio1332 Biochemistry - Lecture Fourteen - Allosteric Enzymes

6 Questions | By Ellycrook | Last updated: Dec 23, 2015 | Total Attempts: 90

Bio1332 Biochemistry - Lecture Fourteen - Allosteric Enzymes

Appreciate that enzyme rates can be altered by various mechanisms. Understand the concept of allostery, and how it might occur in a protein. Discriminate between the different types of inhibitors and their properties. Knowhowquaternarystructurechangesthe properties of an enzyme.

Questions and Answers

1.

Please complete the following sentence:___________ is where a chemical binds to an enzyme away from the active site, influencing the kinetic properties of the enzyme.
2.

What is the average size of an enzyme?
- A.
  
  300 amino acids
- B.
  
  30 amino acids
- C.
  
  200 amino acids
- D.
  
  20 amino acids
3.

Please complete the following sentences (separate your answers with commas):An ________________ is any molecule that can bind to an enzyme away from the active site, and by doing so change the enzyme's activity for its substrate. These effectors can either increase the rate of reaction (named __________________), or reduce the rate of reaction (named _______________).
4.

Please complete the following sentence:An __________ is any molecule that acts to reduce the rate of an enzymatic reaction.
5.
Please fill answer below:
- Many enzymes are made from more than one protein chain (quaternary structure).
- The chains can be identical or different.
- In some cases, the binding of substrate to one subunit (chain) influences the binding to other subunits.
- This results in ___________ between the subunits.

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