Terms : Hide Images
| 4858838283 | Enzymes | Proteins that speed up chemical reactions GREATLY! Functional proteins; their names usually end in - ase Proteins that function as biological catalysts Do not change in the course of a reaction |  | 0 |
| 4858992357 | Enzyme specificity | Only one enzyme for one substrate (complimentary shape). Enzymes are designed to work only on a specific substrate or group of closely related substrates. The unique fitting of the enzyme with its substrate. |  | 1 |
| 4858849371 | Activation energy | Energy required to start a reaction |  | 2 |
| 4858859237 | Environmental factors that influence enzymatic activity | pH, temperature, and salinity | 3 | |
| 4858864271 | Denaturation | A change in the active site which causes the substrates not being to bond anymore. A process in which a protein unravels, losing its specific structure and hence function; can be caused by changes in pH or salt concentration or by high temperature. Also refers to the separation of the two strands of the DNA double helix, caused by similar factors. A change in structure that makes an enzyme nonfunctional. |  | 4 |
| 4858895001 | Active site | catalytic site and binding site together Region of an enzyme into which a particular substrate fits. |  | 5 |
| 4858903145 | Allosteric site | A site on an enzyme other than the active site, to which a specific substance binds, thereby changing the shape and activity of the enzyme. |  | 6 |
| 4858914148 | Competitive inhibition | Inhibition of an enzyme's ability to catalyze a chemical reaction via a non-reactant molecule that competes with the substrate(s) for access to the active site. substance that resembles the normal substrate competes with the substrate for the active site |  | 7 |
| 4858927555 | Noncompetitive inhibition | Also known as allosteric inhibition. Inhibitor molecule binds with allosteric site of enzyme, inducing a change in active site (or blocking active site) |  | 8 |
| 4859002238 | Cofactors | Small, inorganic chemicals. Nonprotein molecules that assist enzymes. activates enzymes by altering the active site of the protein to accept the substrate molecule |  | 9 |
| 4859010523 | Coenzymes | Organic compounds. An organic molecule that is a necessary participant in some enzymatic reactions; helps catalysis by donating or accepting electrons or functional groups; e.g., a vitamin, ATP, NAD+. |  | 10 |
| 4859247665 | Cofactors, coenzymes, and inhibitor analogy | The enzyme is this guy at the club trying to get with this girl (who will represent the substrates). The cofactors and coenzymes are his wingmen, aiding in this process. An inhibitor, however, is a total cock block. A competitive inhibitor is the ugly girl who tries to get with him, competing for the active site, which, in this case, will be represented by the D. A noncompetitive inhibitor in an inhibitor who doesn't wish to bind to the active site. For example, a cop who drags him away from the girl would be a noncompetitive inhibitor because he is still cock blocking (or preventing the sex, or the reaction, from taking place), but he is not competing for the D. | 11 | |
| 4859025982 | Allosteric activator | Binds to allosteric site and increases enzyme activity. An allosteric activator will bind to an enzyme and induce its active form. |  | 12 |
| 4859040493 | Substrates | Molecules at the beginning of the chemical reaction process. The substances that enzymes act upon. |  | 13 |
| 4859061553 | Michael-Menten constant | The amount of substrate needed to reach a given rate of reaction. | 14 | |
| 4859079054 | Enzyme's primary structure | A long sequence of amino acids that bond with one another. |  | 15 |
| 4859088743 | Enzyme's secondary structure | Short range interactions between amino acids can be alpha-helix or beta sheet. Alphas look like spirals, betas look like flat, wavy sheets. |  | 16 |
| 4859104383 | Enzyme's tertiary structure | The long range interactions when amino acids interact with other amino acids a long way down the strand, and as they fold over, they form a globular structure. |  | 17 |
| 4859114784 | Enzyme's quaternary structure | One globular strand interacts with other tertiary pieces. When bonds are formed at this level, they are usually hydrogen bonds, but sometimes it's two hydrophobic pieces interacting, or even ionic bonds. When an enzyme is unfolded, it's referred to as being denatured. |  | 18 |
| 4859396608 | Rate of reaction | How rapidly or slowly a reaction occurs. |  | 19 |
| 4859407426 | Substrate concentration | As the substrate concentration increases, so does the rate of reaction, until all of the active sites are bound and the rate of reaction levels off. |  | 20 |
| 4859412373 | Enzyme concentration | The greater concentration of the enzyme the greater the rate of reaction. |  | 21 |
