3. How does changes in enzymatic factors affect the native conformation of enzymes? What happens to the enzyme's native conformation once it is denatured? What structural organization are destroyed by this process?

8.Choose the False statement about enzyme binding sites Binding at an allosteric site ca affect binding and catalysis at the Ortho steric site. In addition to ortho steric sites , some enzymes have other sites where catalysis can be conducted. They are called , allosteric sites, from “allo,” the other. In principle, allosteric ligands can have structures that do not resemble those of substrates. Ligand binding at an allosteric site can cause a conformational change of an enzyme. Enzyme can be inhibited by an allosteric ligand that does not complete with substrate.

7. As far as location, where do each of these metabolic reactions occur in a eukaryote? A prokaryote? Why the difference?

1.  Which of the following are general properties of active sites?  MARK ALL THAT APPLY. Group of answer choices Multiple interactions with substrate Not very specific Always hydrophobic Small pocket within enzyme.

3. Which of the following statements regarding enzymes and transition states is true? a. stabilization of the transition state must be less than stabilization of ES for catalysis to occur b. binding of substrate to an enzyme often causes strain, thus promoting transition state formation c. the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state d. formation of the transition state always assures that the reaction will proceed to product e. none of the above are true 4. What is the starting point for selection of a suitable ion-exchange chromatography matrix for purification of a recombinant protein? a. Prediction of isoelectric point (pl) from the amino acid sequence. b. Test protein binding to an ion-exchange matrix at a range of pHs and salt concentrations. c. Test protein binding to a selection of anion and cation exchange matrices. d. Pass your sample through a preparative column and elute with a…

2. How do enzymes catalyze a metabolic reaction (Substrate and enzymes). Giveone metabolic reaction in a chemical equation form.

6. What is a glycosyltransferase? Choose all that apply Group of answer choices Catalyzes the formation of a bond between a sugar and an amino acid An enzyme that cleaves a glycosidic bond An enzyme that catalyzes the formation of a glycosidic bond An enzyme that transfers nucleotide-sugars from the cytoplasm   7.  Which statement(s) is/are true about inverting and retaining glycosyltransferases?  a. Inverting glycosyltransferase catalyzes the epimerization of a sugar b. Inverting glycosyltransferase alters the anomeric configuration of the glycosyl donor c. Retaining glycosyltransferase never preserves the anomeric configuration of the glycosyl donor d. Inverting glycosyltransferase switch the order of acceptor and donor. e. An SN1 reaction mechanism results in exclusive retention of stereochemistry of the anomeric carbon