AP- Biology - Enzymes Flashcards
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7848535770 | chemical reaction | A process that changes one set of chemicals into another set of chemicals. | ![]() | 0 |
7848535771 | reactants | compounds that enter into a chemical reaction | ![]() | 1 |
7848535772 | product | compounds produced by a chemical reaction. | ![]() | 2 |
7848535773 | enzyme | biological catalysts usually globular that speed up the rate of chemical reactions | ![]() | 3 |
7848535774 | coenzyme | A non protein organic molecule serving to modify the active site of an enzyme before the reaction is allowed to occur. Most vitamins function important metabolic reactions in this role. | ![]() | 4 |
7848535775 | Competitive inhibition | substance that resembles the normal substrate competes with the substrate for the active site | ![]() | 5 |
7848535776 | Noncompetitive inhibitor | a chemical that binds to an enzyme but not in the active site. This chemical will change the shape of the enzyme (reversible) | ![]() | 6 |
7848535777 | substrate | the substance an enzyme catalyzes, changes. | ![]() | 7 |
7848535778 | active site | the location on the enzyme where the substrate binds and goes through a chemical reaction. | ![]() | 8 |
7848535779 | exothermic reaction | a chemical reaction where energy is given off, so that the products have less energy than the reactants. | ![]() | 9 |
7848535780 | endothermic reaction | a chemical reaction where energy is taken in, so that the products have more energy than the reactants. | ![]() | 10 |
7848535781 | activation energy | Eₐ is the abbreviation used for the energy required to start a reaction. | ![]() | 11 |
7848535782 | sucrase | An enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose | ![]() | 12 |
7848535783 | Catalase | an enzyme found in most aerobic organisms that breaks down H2O2 to water and oxygen | ![]() | 13 |
7848535784 | amylase | Enzyme that can break the bonds of starch to form the carbohydrate monomer, glucose. | ![]() | 14 |
7848535785 | lipase | Enzyme that can break the bonds of lipids to form the monomer, fatty acids. | 15 | |
7848535786 | protease | Enzyme that can break the polypeptide bonds of proteins to form the monomer, amino acids. | 16 | |
7848535787 | nuclease | Enzyme that can break the bonds of nucleic acids to form monomer, nucleotides | 17 | |
7848535788 | activated complex | the structure that is made up of the substrate bonded to the active site of the enzyme. | ![]() | 18 |
7848535789 | lock and key hypothesis | The substrate fits the active site of the enzyme like a key fits in a lock. There is no change to the shape of the enzyme or substrate. | ![]() | 19 |
7848535790 | induced fit hypothesis | The active site of the enzyme is flexible and conforms to fit the substrate like a glove fits on a hand. | ![]() | 20 |
7848535791 | Denature | Characteristic of proteins; a change in shape that stops the protein from functioning. | ![]() | 21 |
7848535792 | Allosteric | __________ regulation of enzyme occurs when a molecule binds to an enzyme changing the protein's shape | ![]() | 22 |
7848535793 | Catalyst | ______ an agent that speeds up a chemical reaction without itself being permanently altered | 23 | |
7848535794 | G | An exergonic reaction releases free energy. The abbreviation for free energy is: Named after the American Scientist Josiah Gibbs | 24 | |
7848535795 | Transition State | The less stable state that occurs and is usually a high-energy state between reactants and products in a chemical reaction | 25 | |
7848535796 | Inducing Strain | The enzyme cause bonds in the substrate to stretch | ![]() | 26 |
7848535797 | Substrate orientation | When Enzyme bring together specific atoms into a correct position that are otherwise rotating and tumbling so that bonds can form | 27 | |
7848535798 | Side chain (R group) | the part of the enzyme that can add H+ ions to or from substrate destabilizing covalent bonds | 28 | |
7848535799 | Metal | __________ ions such as Copper, Zinc iron bind to certain enzymes to initiated chemical reactions. | 29 | |
7848535800 | Heme | Organic molecules with iron an iron cofactor (A Prosthetic Group) that are permanently bond to enzyme responsible Oxygen transport | 30 | |
7848535801 | Irreversible Inhibition | When an enzyme inhibitor that covalently binds to the amino acid side chain at the active site of an enzyme it is called _______________ | ![]() | 31 |
7848535802 | Reversible Inhibition | When an enzyme inhibitor binds is similar to the substate and non-covalently bind to the active site and there slows down the enzyme | 32 | |
7848535803 | Protein Kinases | enzymes that reversibly activate or inactivate other proteins by adding phosphate groups to (phosphorylating) them | 33 | |
7848535804 | Activator | A non-covalent binding regulator that can cause an enzyme to change shape and expose and expose an otherwise unexposed active site in allosteric regulation | 34 | |
7848535805 | Shape | in Biology the prefix allo means "different" and stereos means "__________" | 35 | |
7848535806 | Hydrogen | The specificity and activity of an enzyme depends on it 3D structure and this in turn depends on ______________ bonds | 36 | |
7848535807 | hydrophobic | Changes in H+ ions (acidity) concentration can alter how _____________ some regions of protein are. | 37 | |
7848535808 | pH | After looking at the graph the enzyme activity of the the three different enzymes is being regulated by what variable | ![]() | 38 |
7848535809 | Temperature | After looking at the shape of graph the enzyme activity of this enzymes is being regulated by what variable: | ![]() | 39 |
7848535810 | Substrate Concentration | After looking at the shape of graph the enzyme activity of this enzymes is being regulated by what variable: | ![]() | 40 |