5-Biochemistry-生物化学.ppt

Regulatory Strategies: Enzymes and Hemoglobin The activity of proteins, including enzymes, often must be regulated so that they function at the proper time and place. The biological activity of proteins is regulated in four principal ways: Allosteric control. Allosteric proteins contain distinct regulatory sites and multiple functional sites. Multiple forms of enzymes. Isozymes are homologous enzymes within a single organism that catalyze the same reaction but differ slightly in structure Reversible covalent modification. The catalytic properties of many enzymes are markedly altered by the covalent attachment of a modifying group, most commonly a phosphoryl group. Proteolytic activation. Many enzymes are activated by the hydrolysis of a few or even one peptide bond in inactive precursors called zymogens or proenzymes. Aspartate Transcarbamoylase Is Allosterically Inhibited by the End Product of Its Pathway Hemoglobin Transports Oxygen Efficiently by Binding Oxygen Cooperatively Isozymes Provide a Means of Regulation Specific to Distinct Tissues and Developmental Stages Covalent Modification Is a Means of Regulating Enzyme Activity Many Enzymes Are Activated by Specific Proteolytic Cleavage Summary Aspartate Transcarbamoylase Is Allosterically Inhibited by the End Product of Its Pathway Hemoglobin Transports Oxygen Efficiently by Binding Oxygen Cooperatively Isozymes Provide a Means of Regulation Specific to Distinct Tissues and Developmental Stages Covalent Modification Is a Means of Regulating Enzyme Activity Many Enzymes Are Activated by Specific Proteolytic Cleavage Carbohydrates Carbohydrates are aldehyde or ketone compounds with multiple hydroxyl groups. They make up most of the organic matter on Earth because of their extensive roles in all forms of life. First, carbohydrates serve as energy stores, fuels, and metabolic intermediates. Second, ribose and deoxyribose sugars form part of the structural framework of RNA and DNA. Third, polysaccharide