enzymes p2 nucleotides 1,2 finals Flashcards
(100 cards)
three types of specificity enzymes
stereochemical, reaction, substrate
only one of the isomers which acts as a substrate for an enzyme action
optical specificity
specific to only one isomer even if the compound is one type of molecule
stereospecificity
one enzyme can catalyze only one of the various reactions
reaction specificity
one enzyme catalyzes or acts on only one substrate
absolute specificity
enzymes that catalyze similar molecules with the same functional group (trypsin and chymotrypsin)
group specificity
observed in proteolytic enzymes, glycosidases, and lipases which act on peptite bonds, glycosidic bonds and ester bonds
bond specificity
enzyme is most active on its optimum temperature
effect of temperature
enzymatic reaction depends on the pH of the medium
effect of pH
enzymatic reaction is directly proportional to the enzyme concentration
effect of enzyme concentration
products formed as a result of enzymatic reaction may accumulate, and this excess of product may lower the enzymatic reaction by occupying the active site of the enzyme.
effect of product concentration
reaction is directly proportional to the substrate concentration, but only true up to a certain concentration after which the increasing concentration of substrate does not further increase the velocity of the reaction
effect of substrate concentration
Certain enzymes is dependent on metal ion activators and coenzymes
effect of activators and coenzyme
Whenever the active site is not available for binding of the substrate, the enzyme activity may be reduced.
effect of modulators and inhibitors
Time required for completion of an enzyme reaction increases with decreasing temperature from its optimum.
effect of time
the lock is the enzyme and the key is the substrate. Only the correctly sized key (substrate) fits into the key hole (active site) of the lock (enzyme
lock-and-key model
he postulated the lock-and-key model in 1894
Emil Fischer
the substrate plays a role in determining the final shape of the enzyme and that the enzyme is partially flexible.
induced fit model
he created the induced fit model in 1958
Daniel E. Koshland, Jr.
These enzymes contains active sites with catalytic residues that can form temporary covalent bonds with the substrate molecules.
covalent catalysis
These implies that for the reaction to occur, they must be close enough and must also have the proper orientation.
catalysis by proximity and orientation
Active sites may contain residue such as histidine that can participate in hydrogen ion transfer.
acid-base catalysis
Metal atoms such as Zinc, Magnesium and Iron are used as cofactors by a multitude of different enzymes.
metal-ion catalysis
Rates of enzyme-catalyzed reactions can be decreased by a group of substances called inhibitors.
enzyme inhibition