C5-controlofenzymeactivity.ppt

3.2 Protein kinases catalyze the transfer of a phosphate group from an ATP molecule to the side chains of Ser, Thr, or Tyr residues in proteins. 3.3 Protein phosphatases catalyze the hydrolysis of phosphoryl groups attached to proteins, thus reversing the effects of kinases. 3.4 The degree of specificity of protein kinases varies. Some catalyze the phosphorylation of many different target proteins (at sites of conserved sequences, e.g., protein kinase A recognizes a conserved sequence made of Arg-Arg-X-Ser-Z or Arg-Arg-X-Thr-Z). Some phosphorylate a single protein or several closely related ones. 3.5 Phosphorylation is a highly effective means of controlling the activity of proteins for structural, thermodynamic, and kinetic reasons. Regulation of glycogen phosphorylase activity Glucose (red), AMP (dark blue, allosteric activator), pyridoxal phosphate (PLP, B6 derivative, light blue), and ser14 (yellow) Glycogen phosphorylase 磷酸化 腺苷酰化 尿苷酰化 糖基化 甲基化 4. Many enzymes are activated by specific proteolytic cleavage 4.1 These enzymes are synthesized as inactive precursors called zymogens or proenzyme. 4.2 They are activated by cleavage of one or several specific peptide bonds. 4.3 Proteolytic activation, in contrast with allosteric control and reversible covalent modification, can occur just once in the life of the enzyme molecule. 4.4 The digestive enzymes that hydrolyze proteins are synthesized as zymogens in the stomach and pancreas. 4.5 Blood clotting is mediated by a cascade of proteolytic activation. 4.6 Some protein hormones are synthesized as inactive precursors (e.g., insulin is derived from proinsulin by proteolytic removal of a peptide). 5. Both the synthesis and degradation of the certain important enzymes are tightly controlled 5.1 Amount of some enzymes are increased when certain inducers (often enzyme substrates) are present in the cells. This is often seen in bacterium cells. 5.2 The presence of lactose 乳糖 in a culture medium induces a large increase