生物化学资料：5-Enzyme.pptVIP

UNIT I Protein Structure and Function第一单元 蛋白质的结构和功能 Chapter 5 Enzymes 第5章 酶 non-competitive inhibitors bind some-where other than the active site, and these bindings reduce the speed at which the enzyme runs, reducing the apparent Vm. Km is unaffected, because for a non-competitive inhibitor, Ki = Kis, and if you run the maths, this results in no apparent change to Km. DIPF (diisopropylphosphofluoridate)二异丙基磷酸氟 β-内酰胺类抗生素都能抑制胞壁粘肽合成酶，即青霉素结合蛋白（penicillin binding　proteins，PBPs），从而阻碍细胞壁粘肽mucopeptide合成，使细菌胞壁缺损，菌体膨胀裂解。 肾素—血管紧张素—醛固酮系统（RAS)在高血压发生、发展中起重要作用，其中血管紧张素Ⅱ是主要的效应肽。ACEI抑制血管紧张素Ⅰ转换为血管紧张素Ⅱ，不灭活缓激肽，产生降压效应。 尿素（水解反应）：用H+ (催化剂)，６２（所需温度），７.４×１０-7（速率常数）。用脲酶(催化剂)， ２１ （所需温度）， ５.０×１０6 （速率常数）。 proximity effect orientation arrange(邻近效应与定向排列); surface effect desolvation(表面效应与脱溶剂化); three-dimensional structure three-dimensional structure two major classes of regulatory enzymes (1) Allosteric enzyme : function through reversible, noncovalent binding of regulatory compounds →effectors or allosteric modulator, also be called as ligand of enzyme(small metabolites, cofactor, or substrate self…) activator (positive), inhibitor (negative) (2) Other enzyme : reversible covalent modification VIII-A. Allosteric binding sites Allosteric enzymes are generally large complex, having the regulatory subunits the catalytic subunits. Allosteric enzymes noncovalently bind effectors at a site other than the active site. The substrate binding site the effector binding site are usually on different subunits. Binding of effectors causes conformational change of E. VIII-A-1. Homotropic effectors Allosteric enzymes are multi-subunit enzymes, showing a cooperative response to substrates as well as to modulators, resulting in sigmoid kinetics. Homotropic(同协同)means one molecule influences the binding of a second similar molecule. When the substrate itself acts as an allsteric effector, the effect is said to be homotropic, usual