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| 6314746626 | Primary structure | amino acid sequence | 0 | |
| 6314774911 | hydrolase | hydrolyzes chemical bonds (Atlases, proteases) | 1 | |
| 6314777422 | Isomerase | rearranges bond within a molecule to form an isomer | 2 | |
| 6314781498 | Ligase | forms a chemical bond (DNA ligase) | 3 | |
| 6314783816 | Lyase | break chemical bonds by means other than oxidation or hydrolysis (pyruvate decarboxylase) | 4 | |
| 6314790537 | Kinase | transfer a phosphate group to a molecule to a molecule from a high energy carrier, such as ATP (phosphofructokinse PFK) | 5 | |
| 6314797698 | Oxidoreductase | runs reduce reactions | 6 | |
| 6314801670 | Polymerase | polymerization (addition of nucleotides to the leading strand of DNA by DNA polymerase) | 7 | |
| 6314804334 | Phosphatase | removes a phosphate group from a molecule | 8 | |
| 6314817453 | Protease | hydrolyzes peptide bonds | 9 | |
| 6314842582 | Competitive inhibitors | -compete with substrate for the active site -Vmax is not changed -Km is increased, because you can overcome the inhibitor by increasing the amount of substrate - the affinity is decreased because it takes more substrate to reach Km -Think of it as a alcoholic versus freshman The alcoholic is going to take a lot longer to get drunk because his tolerance is increased (Km increased), thus his receptors are less sensitive, his affinity has decreased A freshman who doesn't drink, will only need a few beers to get drunk (Km) so the Km is decreased, thus the freshman has more affinity for the alcohol from one beer. |  | 10 |
| 6314895703 | Non competitive inhibitor | -Inhibitor can bind to the enzyme with or without the substrate bond to it -Vmax is decreased because the amount of functional ES complexes is decreased. -the substrate can bind without any problems, so Km does not change | | 11 |
| 6315017462 | Uncompetitive inhibition | -Inhibitor binds the to allosteric site of the ES complex and does not allow the product to be made. -Reduces the number of functioning ES complexes, thus reduces product -Vmax is decreased -Km has decreased, the affinity has increased, the enzyme complex has such a high affinity for the substrate that it will not leave the active site of the enzyme complex On the plot,it is opposite of what you say since its the inverse. |  | 12 |
| 6315255331 | Line weaver-Burke Plot | slope: Km/Vmax y-intercept: 1/vmax x-intercept: -1/Km ** Increase in substrate concentration means a decrease in the value along the x-axis because it is the inverse ** increase the reaction rate V is a decrease in the inverse of the reaction , so reaction rate increases, the value along the y-axis decreases. |  | 13 |
| 6315306695 | Bronsted-Lowry Acids and bases | BAD Bronsted, Acid, Donates Acid: Protons (H+) donors Base: Proton (H+) accepters |  | 14 |
| 6315330449 | Oxidation Reaction Reduction Reaction | Oxidation: Gain of oxygen molecule, loss of hydrogen atoms, loss of electrons Reduction: is the opposite of oxidation | 15 | |
| 6315342432 | Exergonic Endergonic | Negative Delta G Postive Delta G | 16 | |
| 6315342433 | Ka value pka value | -the larger the Ka the stronger the acid; the smaller the Ka value, the weaker the acid -lower pka, stronger the acid, easily deprotonated -pH greater than pka, acid is deprontonated (basic solution) | 17 | |
| 6315393392 | Secondary structure | Hydrogen bonds between back bond, Proline kinks for beta sheets, and alpha helix | 18 | |
| 6315398089 | Tertiary structure | hydrophobic and hydrophilic interactions between amino acids residues located more distantly from each other in the polypeptide chains. | 19 | |
| 6315410854 | Quaternary structure | various bonds between separate chains | 20 | |
| 6315575959 | Vmax | Constant, it depends on enzyme concentration and what enzyme you have. Vmax is when all substrates are fully saturated, when enzymes are attached to active site all the time | 21 | |
| 6315601515 | Km | How much substrate you need to have in order to make 1/2 vmax -measure of the enzymes affinity for that specific substrate -Km low, the enzyme has a high affinity for that substrate -Km high, the enzyme does not have a high affinity for that substrate (drink a lot, need more alcohol to get buzz) | 22 | |
| 6331065151 | Periodic table trends | 23 |
