| A | B |
| non-enzymatic glycosylation | --- |
| Proteases | Cleave the backbone by targeting a protein |
| What does a protease use to target a protein? | Ubiquitin |
| Where does a protease target a protein? | Lysine Residue |
| What is the protein chopping factory called? | Proteosome |
| A biotech company is developing a ubiquitin ligase inhibitor for the treatment of cancer. This drug would increase protein | Half-Life |
| Association Constant | Ka |
| Ka= | kon/koff= [PL]/[P][L] |
| Kd is used to measure what? | binding Strength |
| Kd= | [P][L]/[PL]=1/Ka |
| Kd is concentration at which binding is what? | Half Saturation |
| Low Kd means | very specific |
| slide 42 | 42 |
| Enzymes affect activation energy and reaction rate, How? | Lower, Increase |
| OIL RIG | Oxidation and reduction |
| NAD and FAD | Redox cofactors, electron acceptors and donors |
| slide 51 memorize | 51 |
| V= | velocity-> how much Product is produced |
| Km | concentration of substrate needed to reach one half Vmax |
| Km | measure of the affinity of the substrate for the enzyme (how well the substrate binds in the active site) |
| Michaelis-Menten | Vi= Vmax[S]/Km+[S] |
| FAD | Riboflavin (B2) Redox |
| A patient with elevated blood glucose is diagnosed with a rare form of diabetes caused by a mutation in the enzyme glucokinase. Based on the graph, this mutation alters | Substrate Binding |
| NAD | Niacin (B3), Redox |
| TPP | Thiamine (B1), Oxidative Decarboxylation |
| CoA | Pantothenate (B5), Acyl group Transfer |
| Biotin | Biotin (Carboxylation) |
| Tetrahydrolate | Folic Acid, One carbon group transfer |
| Pyridoxal Phosphate | Pyridoxine (B6), Transamination |
| The table below provides information on GLUT transporters which are responsible for import of glucose into cells. Which tissue is most likely to be using glucose for energy when blood glucose concentration is low? | whichever has the lowest Km |
| Competitive enzyme inhibitors bind where? | same site as substrate |
| Compeitive enzyme inhibitors do what to apparent Km and velocity? | Does not chang evelocity, but does change apparent Km |
| Which type of inhibition can be overcome? | Competitive inhibition |
| Noncompetitive Inhibitors | do not bind same site as substrate |
| Noncompetitive inhibitors do what to Km and Vmax? | Km is not altered but Vmax decreases |
| Noncompetitive inhibitors | can not be overcome by increased concentration |
| antagonist | Naloxone |
| agonist | morphine |
| block signal | antagonist |
| Allosteric inhibition and activation | important for self regulation of metabolic pathways and maintenance of energy homeostasis |
| practice slide 67 | 67 |