第八章酶通论.pptVIP

第八章 酶学通论 王顺昌 In all living organisms, thousands of chemical reactions are proceeding very rapidly at any given instant. Virtually all of these reactions are mediated by enzymes—proteins specialized to catalyze metabolic reactions. Many reactions, such as glucose oxidation, take place rapidly in the living organisms. The enzyme play crucial roles to accelerate and control the rates of the reactions. Biological catalysis was first recognized and described in the late 1700s. In the 1850s, Louis Pasteur concluded that fermentation of sugar into alcohol by yeast is catalyzed by “ferments.” Then in 1897 Eduard Buchner discovered that yeast extracts could ferment sugar to alcohol. In 1878，Frederick W. Kühne called these molecules enzymes. In 1913，Mechaelis and Menten proposed MM function The isolation and crystallization of urease by James Sumner in 1926. In 1930s, John Northrop and Moses Kunitz crystallized pepsin, trypsin, and other digestive enzymes and found them also to be proteins. In early 1980s, Cech and Altman found ribozyme 第一节 酶催化作用特点 一、酶和一般催化剂比较：增加反应速率，加快达到化学平衡，但不改变反应常数。 在化学反应体系内，只有处于活化状态的分子才能在分子碰撞中发生化学化应。分子活化需要活化能 (activation energy)，定义为，在一定温度下，1mol底物全部进入活化态所需要的自由能(free energy)。过氧化氢分解所需活化能为75.4kJ/mol, 用液态钯作催化剂降低为48.9 4kJ/mol，而过氧化氢酶时为8.4kJ/mol. 二、酶作为催化剂的特点 1. 高效性：Catalytic power is defined as the ratio of the enzyme-catalyzed rate of a reaction to the uncatalyzed rate. Urea + 2H2O + H+ 2NH4+ +HCO3- at 20 Celsius degree, urease-catalyzed reaction constant is 3x104/sec, while the uncatalyzed reaction constant is 3x10-10/sec, so the catalytic power is 1014.p321 TAB 通常使用酶的转换数(kcat)表示酶的催化效率，定义为每秒钟每个酶分子转换底物的分子数，或每微摩尔酶分子转换底物的微摩尔数。一般为每秒1-10000 2. Specificity is defined as the abilities to select the substrates as well as products,such as urease, DNA polymerase etc.通常一种酶只能催化一种或一类反应，作用于一种或一类物质。 Substrates refer to the substances upon which an enzyme acts. No nonproductive side reactions, no wasteful byproducts. 3. Regulation-enzyme-catalyzed re