Question | Answer |
neg. delta G leads to what kind of reaction? | favorable |
do enzymes change the delta G of a reaction? | no |
at what point in a reaction do substrates have their highest energy level? | transition point |
what must happen to glucose before it can enter a cell? | hexokinase must phosphorylate it |
why isn't galactose a good substrate? | bad stereochemistry |
in acid-base catalysis, which amino acid side chain is most likely used? | histidine |
what is the optimum ph range for chymotrypsin? | above the pka |
aside from histidine, what protease uses acid-base catalysis? | aspartic proteases |
where are aspartic proteases found in cells? | lysosomes |
give an example of an oxidoreductase? | ADH |
what does an activation transfer coenzyme do? | transfers functional groups from one molecule to another |
NAD and FAD are examples of what? | redox coenzymes |
NAD is synthesized from what vitamin? | niacin |
FAD is synthesized from what vitamin? | riboflavin |
is NAD a coenzyme or a substrate? | both |
what is important for maintaining redox balance? | glutathione (reduced) |
give examples of activation transfer coenzymes: | pyrophosphate, coa, biotin, pyridoxal phosphate |
what reaction type is FAD? NAD? | both are redox reactions |
TPP is what vitamin? | thiamine (B1) |
CoA is what vitamin? | pantothenate (B5) |
what is km? | concentration of substrate needed to reach 1/2 vmax |
would competitive inhibition affect km or vmax? | km |
in noncompetitive inhibition, what is changed? | vmax |
what kind of molecule acts at a site other than the active site? | allosteric |
noncompetitive inhibition does or does not alter the reaction km? | does not |
what inhibition is frequently seen in multisubstrate enzymes? | noncompetitive inhibition |
which inhibition is rare? what is changed | uncompetitive inhibition, km and vmax |
give an example of nonspecific enzyme inhibition: | nonoptimal ph, temperature |