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Which three amino acid residues can be phosphorylated by kinases? What property do these amino acids share that make them targets for phosphorylation? How does phosphorylation of these amino acids alter their chemical properties?

Which three amino acid residues can be phosphorylated by kinases? What property do these amino acids share that make them targets for phosphorylation? How does phosphorylation of these amino acids alter their chemical properties?

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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**Title: Understanding Phosphorylation of Amino Acid Residues** **Question:** Which three amino acid residues can be phosphorylated by kinases? What property do these amino acids share that make them targets for phosphorylation? How does phosphorylation of these amino acids alter their chemical properties? **Explanation:** In biological systems, phosphorylation is a key post-translational modification that regulates protein function and signaling pathways. This process involves the addition of a phosphate group (PO₄³⁻) to an amino acid residue in a protein, catalyzed by enzymes known as kinases. **Key Amino Acids Involved:** 1. **Serine** 2. **Threonine** 3. **Tyrosine** **Shared Property:** The reason these three amino acids are prime targets for phosphorylation lies in the presence of a hydroxyl (-OH) group in their side chains. This functional group enables the covalent addition of a phosphate group, significantly impacting the protein's function and activity. **Effects of Phosphorylation:** Phosphorylation introduces a negative charge to the amino acid residue, which can lead to a conformational change in the protein structure. These changes may: - Alter the protein's activity - Modify its interactions with other proteins or molecules - Influence its stability and location within the cell Overall, phosphorylation is a crucial mechanism for regulating cellular processes and responding to environmental signals.
Transcribed Image Text:**Title: Understanding Phosphorylation of Amino Acid Residues** **Question:** Which three amino acid residues can be phosphorylated by kinases? What property do these amino acids share that make them targets for phosphorylation? How does phosphorylation of these amino acids alter their chemical properties? **Explanation:** In biological systems, phosphorylation is a key post-translational modification that regulates protein function and signaling pathways. This process involves the addition of a phosphate group (PO₄³⁻) to an amino acid residue in a protein, catalyzed by enzymes known as kinases. **Key Amino Acids Involved:** 1. **Serine** 2. **Threonine** 3. **Tyrosine** **Shared Property:** The reason these three amino acids are prime targets for phosphorylation lies in the presence of a hydroxyl (-OH) group in their side chains. This functional group enables the covalent addition of a phosphate group, significantly impacting the protein's function and activity. **Effects of Phosphorylation:** Phosphorylation introduces a negative charge to the amino acid residue, which can lead to a conformational change in the protein structure. These changes may: - Alter the protein's activity - Modify its interactions with other proteins or molecules - Influence its stability and location within the cell Overall, phosphorylation is a crucial mechanism for regulating cellular processes and responding to environmental signals.
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