Terms : Hide Images
| 8158774579 | chemical reaction | A process that changes one set of chemicals into another set of chemicals. |  | 0 |
| 8158774580 | reactants | compounds that enter into a chemical reaction | | 1 |
| 8158774581 | product | compounds produced by a chemical reaction. | | 2 |
| 8158774582 | enzyme | biological catalysts usually globular that speed up the rate of chemical reactions |  | 3 |
| 8158774583 | 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 |
| 8158774584 | Competitive inhibition | substance that resembles the normal substrate competes with the substrate for the active site |  | 5 |
| 8158774585 | 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 |
| 8158774586 | substrate | the substance an enzyme catalyzes, changes. | | 7 |
| 8158774587 | active site | the location on the enzyme where the substrate binds and goes through a chemical reaction. |  | 8 |
| 8158774588 | exothermic reaction | a chemical reaction where energy is given off, so that the products have less energy than the reactants. |  | 9 |
| 8158774589 | endothermic reaction | a chemical reaction where energy is taken in, so that the products have more energy than the reactants. |  | 10 |
| 8158774590 | activation energy | Eₐ is the abbreviation used for the energy required to start a reaction. |  | 11 |
| 8158774591 | sucrase | An enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose |  | 12 |
| 8158774592 | Catalase | an enzyme found in most aerobic organisms that breaks down H2O2 to water and oxygen |  | 13 |
| 8158774593 | amylase | Enzyme that can break the bonds of starch to form the carbohydrate monomer, glucose. |  | 14 |
| 8158774594 | lipase | Enzyme that can break the bonds of lipids to form the monomer, fatty acids. | 15 | |
| 8158774595 | protease | Enzyme that can break the polypeptide bonds of proteins to form the monomer, amino acids. | 16 | |
| 8158774596 | nuclease | Enzyme that can break the bonds of nucleic acids to form monomer, nucleotides | 17 | |
| 8158774597 | activated complex | the structure that is made up of the substrate bonded to the active site of the enzyme. |  | 18 |
| 8158774598 | 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 |
| 8158774599 | 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 |
| 8158774600 | Denature | Characteristic of proteins; a change in shape that stops the protein from functioning. |  | 21 |
| 8158774601 | Allosteric | __________ regulation of enzyme occurs when a molecule binds to an enzyme changing the protein's shape |  | 22 |
| 8158774602 | Catalyst | ______ an agent that speeds up a chemical reaction without itself being permanently altered | 23 | |
| 8158774603 | G | An exergonic reaction releases free energy. The abbreviation for free energy is: Named after the American Scientist Josiah Gibbs | 24 | |
| 8158774604 | Transition State | The less stable state that occurs and is usually a high-energy state between reactants and products in a chemical reaction | 25 | |
| 8158774605 | Inducing Strain | The enzyme cause bonds in the substrate to stretch |  | 26 |
| 8158774606 | Substrate orientation | When Enzyme bring together specific atoms into a correct position that are otherwise rotating and tumbling so that bonds can form | 27 | |
| 8158774607 | Side chain (R group) | the part of the enzyme that can add H+ ions to or from substrate destabilizing covalent bonds | 28 | |
| 8158774608 | Metal | __________ ions such as Copper, Zinc iron bind to certain enzymes to initiated chemical reactions. | 29 | |
| 8158774609 | Heme | Organic molecules with iron an iron cofactor (A Prosthetic Group) that are permanently bond to enzyme responsible Oxygen transport | 30 | |
| 8158774610 | 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 |
| 8158774611 | 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 | |
| 8158774612 | Protein Kinases | enzymes that reversibly activate or inactivate other proteins by adding phosphate groups to (phosphorylating) them | 33 | |
| 8158774613 | 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 | |
| 8158774614 | Shape | in Biology the prefix allo means "different" and stereos means "__________" | 35 | |
| 8158774615 | Hydrogen | The specificity and activity of an enzyme depends on it 3D structure and this in turn depends on ______________ bonds | 36 | |
| 8158774616 | hydrophobic | Changes in H+ ions (acidity) concentration can alter how _____________ some regions of protein are. | 37 | |
| 8158774617 | pH | After looking at the graph the enzyme activity of the the three different enzymes is being regulated by what variable |  | 38 |
| 8158774618 | Temperature | After looking at the shape of graph the enzyme activity of this enzymes is being regulated by what variable: |  | 39 |
| 8158774619 | Substrate Concentration | After looking at the shape of graph the enzyme activity of this enzymes is being regulated by what variable: |  | 40 |
