Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

7. Enzyme Inhibition and Regulation

Phosphorylation

Biochemistry

7. Enzyme Inhibition and Regulation

Phosphorylation

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Multiple Choice

Covalent modification of an enzyme usually involves phosphorylation / dephosphorylation of:

Lysine residue.

Proline residue.

Serine residue.

Aspartate residue.

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Verified step by step guidance

Understand the concept of covalent modification: Covalent modification is a regulatory mechanism where enzymes are activated or deactivated by the addition or removal of chemical groups, such as phosphate groups.

Learn about phosphorylation and dephosphorylation: These processes involve the addition (phosphorylation) or removal (dephosphorylation) of a phosphate group, typically mediated by kinases and phosphatases, respectively.

Identify the amino acid residues commonly involved in phosphorylation: Phosphorylation typically occurs on amino acid residues with hydroxyl (-OH) groups in their side chains, such as serine, threonine, and tyrosine.

Analyze the options provided: Lysine and proline do not have hydroxyl groups in their side chains, making them unlikely candidates for phosphorylation. Aspartate has a carboxyl group, not a hydroxyl group, so it is also not typically phosphorylated. Serine has a hydroxyl group, making it a common site for phosphorylation.

Conclude that serine residues are the correct answer: Based on the chemical properties of the amino acids, serine is the residue most commonly involved in covalent modification through phosphorylation or dephosphorylation.