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ALLOSTERIC ACTIVATION AND INHIBITION

-The way a cell can tightly regulate its metabolic pathways is by controlling when and where its
various enzymes are active
-it does this by switching on and off the genes that encode specific enzymes
-it can also regulate the activity of enzymes once they are made
-regulatory molecules change an enzyme’s shape and the functioning of its active site by binding
to a site elsewhere on the molecule via noncovalent bonds

-allosteric regulation= any case in which a protein’s function at one site is affected by the
binding of a regulatory molecule to a separate site, resulting in inhibition or stimulation of an
enzyme’s activity
-alosterically regulated enzymes are constructed from 2+ polypeptide chains or subunits,
each with its own active site
-the entire complex oscillates btwn two conformational states
1)catalytically active
2)catalytically inacitive
-in the simplest of allosteric regulation, activating or inhibiting regulatory molecule binds
to regulatory (allosteric) site located where subunits join
~activator binds stabilizes conformation that has functional active sites
~inhibitor bindsstabilizes the inactive form of the enzyme
-subunits of allosteric enzyme fit together so that a conformational change in one subunit
is transmitted to all others

-fluctuating concentrations of regulators can cause a pattern of response in the activity of cellular
enzymes
-ex: the products of ATP hydrolysis play major role in balancing the flow of traffic
between anabolic and catabolic pathways by their effects on key enzymes
~ATP binds to several catabolic enzymes allosterically, lowering their affinity for
substrate and inhibiting their activity
~ADP however, functions as an activator of the same enzyme b/c a major
function of the catabolism is to regenerate ATP and is ATP production lags
behind its use, ADP accumulates and activates these key enzymes that speed up
catabolism, producing more ATP. If supply of ATP exceeds demand, the reverse
happens
-ATP, ADP, and other related molecules also affect key enzymes in anabolic pathways,
and in this way, allosteric enzymes control the rates of key reactions in metabolic
pathways

-in another kind of allosteric activation…


-substrate molecule binding of one active site may stimulate the catalytic powers of a
multi-subunit enzyme by affecting the other active sites
-if an enzyme has 2+ subunits, a substrate molecule causing induced fit in one subunit
can trigger the same favorable conformational change in all the other subunits of the
enzyme
-what is stated above is called cooperativity= a mechanism that amplifies the response of
enzymes to substrates; one substrate molecule primes and enzyme to accept additional substrate
molecules more readily

FEEDBACK INHIBITION
-When ATP allosterically inhibits an enzyme in an ATP generating pathway, the result is
feedback inhibition, a method of metabolic control
-feedback inhibition= a metabolic pathway is switched off by the inhibitory binding of its end
product to an enzyme that acts early in the pathway
SEE EXAMPLE FIGURE 8.21 IN BOOK

SPECIFIC LOCALIZATION OF ENZYMES WITHIN THE CELL


-in some cases, a team of enzymes for several steps of a metabolic pathway is assembled into a
multienzyme complex. The arrangement controls and speeds up the sequence of reactions, as the
product from the first enzyme becomes the substrate for an adjacent enzyme in the complex, and
so on, until the end product is released
-some enzymes/ enzyme complexes have fixed locations in the cell
-others are structural components of particular membranes
-others are in solution w/in specific membrane enclosed eukaryotic organelles, each with
its own internal chemical environment
~ex: enzymes for cellular respiration found in mitochondira