Enzyme Catalysis Overview | University of Wolverhampton - Edubirdie

University:
University of Wolverhampton
Course:
4PY019 | Pharmacy
Academic year:

2024
Views:

344

Pages:

2
Author:

Sara

Catalase Increases RO chemical reaction without undergoing permanent change Active site Region on enzyme binding substrate or cofactor during reaction Abyzyme Antibody with catalytic activity Isoenzyme Two or more enzymes with different amino acid structures catalyzing the same reaction Allosteric enzyme Molecule altering enzyme activity by inducing conformational change Proteolytic enzymes Enzymes like papain, trypsin, and thrombin breaking peptide bonds Enzymes 20 years half life Enzymes lasting 20 years before half the molecules degrade Chymotrypsin Pancreatic enzyme breaking down dietary proteins Carbondic anhydrase Catalyzes hydration of CO2 from tissues to blood system Amylase Enzyme breaking down food Pepsin Enzyme converting food into energy Glycolysis Metabolic pathway breaking down glucose into pyruvate Biosynthesis Process of creating biological compounds Post translational modification Process altering proteins after translation Controlling gene expression Regulating the synthesis of proteins from genes Nomenclature Naming system for enzymes based on function Enzyme structure Includes active site shape and allosteric sites 1/2 Lock and key model Enzyme-substrate fit without conformational change Induced fit model Enzyme-substrate fit with conformational change Cofactors Inorganic or organic molecules aiding enzyme activity Catalysis and free energy Lowering activation energy for faster reactions Kinetics of an enzyme Measured based on substrate concentration and reaction velocity 2/2

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