Enzymes In The Numan Body Including Classification

Enzymes Functional proteins Can act by themself: Simple enzyme Vitamioorganic molecule that must be obtained from food All enzymes are proteins but not all proteins are enzymes Enzymes-biological catalysts Highly Specific Rate of reaction. Activity can be regulated All enzymes are chiral makes them Specific almost all processes in the body are Controlled by enzymes In the Human Body Chemical reactions are the major activity Thousands of reactions occur Cells are highly specialized Reactions carried out by enzymes Most enzymes are Water Soluble Conditions: 37°C pH-24 Essential body Cannot make the amino acid Catalyst a Substance that speeds up the rate of a chemical reaction but it itself remains unchanged reduces activation energy; lower activation energy Denaturation Enzymes are highly specific Perform one type of reaction with one specific reactant Produce one product with no side reactions Single Cell Most enzymes are globular proteins Specific shape Flexible when one molecule binds leads to shape Change Side chain interactions Globular proteins Water Solvent Enzymes Special Enzymes Reactant molecules "Substrates" Thrombin Catalysis hydrolysis of a peptide bond following the amino acid arginine Products still "products" used in blood clotting Location on enzyme where Chemical reaction takes place ACTIVE SITE Carboxypeptidase A Catalysis hydrolysis of peptide bonds to remove C-terminal amino acids Enzyme name closely reflects info about function Most enzymes have a two-part name name of Substrate type of reaction followed by -ase ex. glucose oxidase, alcohol dehydrogenase Papain -catalyzes hydrolysis of peptide bonds in many locations used as meat tenderizer + Contact lens Cleaner Older Common names may only have one part end in -in Thrombin, trypsin, pepsin - special jobs Enzyme active site only fits specific molecules based on shape + intermolecular forces Lock + Key Model - only a specific key opens a lock (perfect fit) Induced -fit model - part of the Substrate fits precisely into active site. The remaining parts induce a shape change in the enzymes active site to allow enzyme to fit Enzymes are Chiral b/c they are proteins + contain L-amino acids Removal of Hydrogen = Oxidation Fibrinogen -C-N- Enzymes Enzymes are regulated *allows a response to changing conditions Speed of most enzymes is measured by turnover number *most enzymes turn over 10-1000 molecules per second the max # of substrate molecules reached upon by 1 molecule of enzyme in an amount Session ID dutta1130 Enzyme terminology Simple enzyme - one protein is complete enzyme Conjugated enzyme - contains some non-protein part Essential Cofactor (or coenzyme) is the non-protein part (inorganic) Coenzyme is a cofactor that is an organic molecule Apoenzyme is the protein part (inactive by itself) Holoenzyme (apoenzyme + cofactor) is the active form Energy Effect bond in abnormal shape; under "Strain" bond unstable Catalyic effect Ser, His + Asp have the necessary functional groups to react Important! Enzyme-Substrate Complex *Substrate held to active site by intermolecular forces Proximity effect attraction between hydrophobic pockets to get to active site Orientation effect peptide bond is next to the Catalytic Enzymes Classification of Enzymes Oxidoreductases Catalyze oxidation-reduction reactions Must have 2 reactants: one oxidized, one reduced These are the substrate cofactor A(red) + B(ox) --> A(ox) + B(red) Transferases Catalyze transfer of a group from one molecule to another A-B + C --> A + B-C Hydrolases Catalyze the hydrolysis of - digestion of proteins, carbs A-B + H2O --> addition of groups to a double bond Addition or the reverse reaction to eliminate a molecule (H2O, CO2, NH3) to form a double bond isomerization (rearrangement of atoms) of a substrate Only one substrate, one product bonding together of two substrate molecules Reactions generally not favored unless energy is also produced/consumed Release or conversion of AIP ADP