Biochemistry
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 19, Problem 3P

Assessing the Effect of Active-Site Phosphorylation on Enzyme Activity (Integrates with Chapter 15.) The serine residue of isocitrate dehydroenase that is phosphorylated by protein kinase lies within the active site of the enzyme. This situation contrasts with most other examples of coa1ent modification by protein phosphorylation. where the phosphorylation occurs at a sate remote from the active site. What direct effect do you think such active-site phosphorylation might have on the catalytic activity of isocitrate dehydrogcn.ise? (Sec Barford, D., 1991. Molecular mechanisms for the control of enzymic activity by protein phosphorytation. Biochimica et Biophysica Acta 1133:55—62.)

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12. When glutamic acid is heated to 180°C., it loses a molecule of water to form a lactam. The bond that creates the lactam is an amide bond that forms between the amino nitrogen and the carbon of the side chain -COOH group. What is the most reasonable structure for this lactam? (NOTE: The structure of glutamic acid is shown in Question 1.) COOH COOH ا کچھ جو کچھ C D COOH B COOH E COOH
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