Answer
Protein Kinases bind substrate proteins and ATP and transfer a phosphate group from ATP to amino acids with free hydroxyl (-OH) groups like serine,threonine and tyrosine of protein). The products are the phospho protein and ADP. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine amino acid, which has been shown to be involved in ATP binding. In the central part of the catalytic domain, there is a conserved aspartic acid, which is important for the catalytic activity of the enzyme. When a compound resemling ADP ,has no phosphate donating group,bind to the N-terminal side of the protein kinase block it's activity because it has no phosphate group that kinase can transfer to the - OH group containing amino acid of protein. Thus kinase activity of the protein will block.
Work Step by Step
Protein Kinases bind substrate proteins and ATP and transfer a phosphate group from ATP to amino acids with free hydroxyl (-OH) groups like serine,threonine and tyrosine of protein). The products are the phospho protein and ADP. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine amino acid, which has been shown to be involved in ATP binding. In the central part of the catalytic domain, there is a conserved aspartic acid, which is important for the catalytic activity of the enzyme. When a compound resemling ADP ,has no phosphate donating group,bind to the N-terminal side of the protein kinase block it's activity because it has no phosphate group that kinase can transfer to the - OH group containing amino acid of protein. Thus kinase activity of the protein will block.
