中国医科大学《生物化学》课件-Chapter 3 (7) Enzymes.pptVIP

Chapter 3 Enzymes Contents Overview Enzyme kinetics Regulation of enzymes Application of enzymes Section 1 Overview 1.1 Enzymes,p40 Enzymes are biomolecules with catalytic activities, Proteins,or RNAs (ribozymes) Substrate: reactant, starting materials Monomeric enzymes Oligomeric enzymes Multienzyme complex : an integration of several enzymes with various catalytic functions. Multifunctional enzyme or tandem enzyme: a unique peptide has various catalytic functions. Enzymes Biomolecules (proteins or RNA) Catalyze specific chemical reactions. apoenzyme Prosthetic group Cofactor,coenzymes holoenzyme Simple enzymes: urease,ribonucleases,amylase,proteases,lipases Conjugated enzymes:holoenzyme =apoenzyme+coenzyme cofactor,prosthetic group:Metal ions,small organic compounds (vitamin ) Co-enzymes Non-protein molecules that help enzymes function Associate with active site of enzyme Enzyme + Co-enzyme = holoenzyme Enzyme alone = apoenzyme Organic co-enzymes – thiamin, riboflavin, niacin, biotin Inorganic co-enzymes – Mg ++, Fe++, Zn++, Mn++ 1.2 The active site of an enzyme Active site or active center is a region on the surface of the enzyme protein in which the substrate is bound noncovalently and forms an enzyme-substrate complex Essential groups :binding groups and catalytic groups Imidazole,hydroxyl,sulfhydryl,and βor γcarboxyl groups Enzyme-substrate binding Lock-and-key model Induced fit : substrate binding induces a conformational change in the active site . 1.3 Isoenzymes Isoenzyme is defined as the multiple forms of enzymes that catalyze the same reaction ,but differ in molecular structure ,physical properties,and reaction kinetics. LDH (lactate dehydrogenase ): H (heart ) and M (muscle) 1.4.1 Catalytic efficiency Turnover number:the number of substrate molecules converted to product by one enzyme per second (when the enzyme is fully saturated with substrate) Catalytic Power 1.4.2 Specificity Absolute specificity: a specific substrate,a unique reaction ( Ure