7生物技术导论.pptVIP

MD I MD II Principal Components I ATP Hydrolysis by Myosin Serine Protease Melanie B?ttcher Index Definition Digestive enzymes Blood clotting Complement system Serine Protease Cutting of certain peptide bonds in other proteins Activity depends on a set of amino acid residues in the active site of the enzyme Based on nucleophilic attack of the targeted peptidic bond by a serine Serine Amino acid alcohol as residue Digestive enzymes Chymotrypsin, Trypsin, Elastase closely-similar structures different substrate specificities Pancreatic proteases ? proenzymes trypsinogen and chymotrypsinogen ? synthesized in the pancreas and secreted into the lumen of the small intestine Mechanism Active site Trypsinogen-Trypsin loss of six amino acids from one end overall structures remain similar Ca++ for thermal stability Trypsin Trypsin cleaves peptide bonds on the C-terminal side of arginines and lysines ? Alcaline amino acids Activation by enteropeptidase or through protoelyse Optimum pH 7 to 8 Chymotrypsinogen-Chymotrypsin Chain is clipped in four places ? release of 2 dipeptides ? creation of two breaks in the backbone 1-13 segment retained as part of the active enzyme, linked on by a disulfide bond Chymotrypsin Active site: His57-Ser195-Asp102 Chymotrypsin cuts on the C-terminal side of tyrosine, phenylalanine, and tryptophan residues hydrolysis of bonds of leucyl, methionyl, asparaginyl and glutamyl residues. Elastase cuts peptide bonds next to small, uncharged side chains such as those of alanine, serine, valine and threonin cuts collagen Blood Clotting System Cascade of several mechanism Involved Serine Proteases Thrombin Plasmin Factor 10 a Factor 11 b Thrombin Inactivated Prothrombin cleaves into activated Thrombin Thrombins cuts Paraglobuline (= fibrinoplastic substance) and forms the soluble state of it Precipitation by plasmasalt in unsoluble state Serpins Serine Protease Inhibitors inhibit the action of their respective serine protease ? serine protease