The activity of many enzymes is regulated by reversible covalent modifications. Kinases add a phosphate group from an ATP to a specific hydroxyl group on an amino acid residue within an enzyme. Which of the following amino acids can be phosphorylated by a kinase? (Select all that apply) Cys His Tyr Thr Phe Ser Val
Phosphorylation can be seen in Serine, threonine and tyrosine amino acids via phospoEster bond formation.
Histidine also shows phosporylation via phosporamidate bond formation.
The amino acids that can be phosphorylated by a kinase are:
Ser (Serine)
Thr (Threonine)
Tyr (Tyrosine)
His (Histidine)
These amino acids possess hydroxyl (OH) groups on their side chains, which can act as the target for phosphorylation by kinases. Cys (Cysteine), Phe (Phenylalanine), and Val (Valine) do not have hydroxyl groups on their side chains and therefore cannot be phosphorylated by kinases.
The activity of many enzymes is regulated by reversible covalent modifications. Kinases add a phosphate group...
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thats all the information that he gave us to solve the question. Thank you for trying anyways X C E Question 23 1 pts The free-energy changes for the transfer of individual amino acid residues from a hydrophobic to an aqueous environment are given as follows: Amino acid AG of transfer (kJ/mol Proline -0.8 -12.6 Histidine 6.7 Alanine Methionine 14.3 Based on this information, which of these amino acid pairs is MOST likely to be represented in membrane-spanning alpha helices?...
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