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WVSOM Class of 2012 Enzymology

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
Created by: mhassan