Enzymes and Recombinant enzyme technique. docx

Topic: Enzymes and Recombinant enzyme technique. Student: Tran Thi Giang Class: CD 0802 Enzymes. • Definition: E are proteins that participate in cellular metabolic processes with the ability to enhance the rate of reaction between biomolecules. The name and classification of enzymes: Typically, to generate the name of an enzyme, the suffix -ase is added to the name of its substrate (e.g., lactase is the enzyme that cleaveslactose) or the type of reaction (e.g., DNA polymerase forms DNA polymers) A few enzymes discovered before this naming system was devised are known by common names…( ) By the IEC system,there are six broad groups: Group name Type of reaction catalyzed Oxidoreductoase oxidation-reduction Transferase Transfer group of atoms Hydrolase Hydrolysis Lyase Add/remove atoms to/from a double bond Isomerase Rearrange atoms Ligase Combine molecules using ATP • Enzyme compostion: • Apoenzyme: the polypeptid or protein part of enzyme. • Cofactors: A cofactor is a non-protein substance which may be organic, and called a coenzyme. • Final enzyme: cofactor + apoenzyme. Mechanism of enzyme action • Lock and key model: • Induced model: Factors affecting Enzyme action: Temperature • Little activity at low temperature • Rate increases with temperature • Most active at optimum temperatures (usually 37°C in humans) • Activity lost with denaturation at high temperatures Substrate concentration. • Increasing substrate concentration increases the rate of reaction (enzyme concentration is constant) • Maximum activity reached when all of enzyme combines with substrate pH: • Maximum activity at optimum pH • R groups of amino acids have proper charge • Tertiary structure of enzyme is correct • Narrow range of activity • Most lose activity in low or high pH Enzyme inhibitor Inhibitors : .cause a loss of catalytic activity .Change the protein structure of an enzyme .May be competitive or noncompetitive .Some effects are irreversible A noncompetitive inhibitor: .Does not have a structure like substrate .Binds to the enzyme but not active site .Changes the shape of enzyme and active site .Substrate cannot fit altered active site .No reaction occurs .Effect is not reversed by adding substrate Application of Enzyme Application : Enzyme used: Foodprocessing Amylase from fungi and plants Baby food Tripsin [...]... vector: plasmids from bacteria are cut with the same restriction enzyme to produce sticky ends • Formation of recombinant DNA: identification and cloning the insulin DNA and plasmid DNA are mixed together with ligase enzyme the sticky end bases form hydrogen bonds the ligase joins the DNA backbone and a recomninant plasmid is produced -the recombinant plasmid is introduced into bacteria -a transformed.. .Recombinant enzyme technique (ReE) • Difinition: ReE are proteins which are produced by recombinant DNA technique • History of recombinant DNA tachnique: The recombinant DNA technique was first proposed by Peter Lobban, a graduate student, with A Dale Kaiser at the Stanford University Department of Biochemistry • The following is a summary of the process of making recombinant DNA Technique.. . backbone and a recomninant plasmid is produced -the recombinant plasmid is introduced into bacteria -a transformed bacterium is identified -the gene is cloned by the growing bacterium Production of recombinant enzyme technique • alpha-glactosidase • alpha-L-iduronidase • N-acetylgalactosamine-4-sulfatase • Dornase alfa • Glucocerebrosidase . Topic: Enzymes and Recombinant enzyme technique. Student: Tran Thi Giang Class: CD 0802 Enzymes. • Definition: E are proteins that participate. Amylase from fungi and plants Baby food Tripsin Recombinant enzyme technique (ReE) • Difinition: ReE are proteins which are produced by recombinant DNA technique. • History of recombinant DNA. • Enzyme compostion: • Apoenzyme: the polypeptid or protein part of enzyme. • Cofactors: A cofactor is a non-protein substance which may be organic, and called a coenzyme. • Final enzyme: