Term
|
Definition
enzymes that follow Michaelis-Menten kinetics |
|
|
Term
how Michaelis-Menten enzyme action is governed |
|
Definition
simply by mass action; they catalyze when substrate is present |
|
|
Term
the type of enzymes most enzymes in the cell are |
|
Definition
Michaelis-Menten enzymes; not regulated in the cell |
|
|
Term
an effective way to regulate metabolic traffic |
|
Definition
regulating enzyme activity |
|
|
Term
the enzymes that regulate metabolic traffic |
|
Definition
|
|
Term
key features of allosteric enzymes |
|
Definition
-regulation of catalytic activity by environmental signals -kinetics more complex than those of Michaelis-Menten enzymes -quaternary structure with multiple active sites in each enzyme |
|
|
Term
|
Definition
seems to be the step after which the rxn that yields the final product will take place |
|
|
Term
|
Definition
seems to be the final product of a pathway binding reversibly to the committed step to inhibit the rxn |
|
|
Term
depiction of feedback inhibition |
|
Definition
[image]
here, the final product binds to an alternate site on the allosteric enzyme to inhibit the committed step |
|
|
Term
enzymes that catalyze the committed step of metabolic pathways |
|
Definition
allosteric enzymes always do this |
|
|
Term
some molecules allosteric enzymes can recognize to regulate production of the final product |
|
Definition
-inhibitor molecules -stimulatory molecules |
|
|
Term
depiction of a pathway that uses both inhibition and stimulation |
|
Definition
[image]
here, F and I stimulate the production of each other, F inhibits production of itself, I inhibits production of itself, and K inhibits production of both F and I, thus inhibiting production of itself |
|
|
Term
how allosteric enzymes are regulated |
|
Definition
-changes in substrate concentration -other molecules, i.e., non-substrate molecules |
|
|
Term
how Michaelis-Menten enzymes and allosteric enzymes differ in kinetics |
|
Definition
[image]
the curve for allosteric is sigmoidal because it resembles the letter S |
|
|
Term
2 properties unique to allosteric enzymes |
|
Definition
1: regulation of catalytic activity 2: sigmoidal kinetics |
|
|
Term
the kinetics of allosteric enzymes |
|
Definition
sigmoidal (resembles S on a graph) |
|
|
Term
the concerted model or MWC model of allosteric enzyme regulation |
|
Definition
based on several premises -allosteric enzymes have multiple active sites on different polypeptide chains -the enzyme can exist in the R (relaxed, more active) or T (tense, less active) conformation state -all subunits or active sites must be in the same state; no hybrids (this is the symmetry rule) -substrate (S) binds more readily with R form than T form |
|
|
Term
the active sites on allosteric enzymes |
|
Definition
have multiple active sites on different polypeptide chains |
|
|
Term
the 2 conformations or states an allosteric enzyme can be in |
|
Definition
-R (relaxed, active) -T (tense, less active) |
|
|
Term
state of allosteric enzyme when there's no substrate |
|
Definition
R and T states in e'librium, with T being more stable and thus more common |
|
|
Term
|
Definition
the t/r ratio, which is in the hundreds when there's no substrate |
|
|
Term
|
Definition
rule that all the subunits or active sites of an allosteric enzyme be in the same state |
|
|
Term
the form of allosteric enzyme substrates more readily bind to |
|
Definition
|
|
Term
why allosteric enzymes have sigmoidal (S-shaped) kinetics |
|
Definition
because the binding of substrate disrupts the T <--> R e'librium in favor of R |
|
|
Term
|
Definition
accumulation of substrate binding and disrupting the T <--> R e'librium in favor of R
this accounts for the sharp increase in velocity of rxn |
|
|
Term
the physiological significance of cooperativity in allosteric enzymes (accumulation of substrate binding and disrupting the T <--> R e'librium in favor of R) |
|
Definition
allosteric enzymes are more sensitive to changes in substrate concentration near KM than Michaelis-Menten enzymes with the same Vmax |
|
|
Term
|
Definition
rapid increase in enzyme activity above a certain threshold |
|
|
Term
how the T <--> R e'librium of allosteric enzymes is regulated |
|
Definition
regulator molecules, such as positive and negative effectors |
|
|
Term
|
Definition
binds to the R form of an allosteric enzyme at a regulatory site, distinct from the active site, to stabilize it, increasing c'tration of R and making that enzyme more likely to bind with substrate
make allosteric enzyme more sensitive to substrate |
|
|
Term
|
Definition
binds to T form of an allosteric enzyme and stabilizes it, increasing c'tration of T, which makes the R form less likely to bind with substrate
make allosteric enzyme less sensitive to substrate |
|
|
Term
|
Definition
effects of regulatory molecules on allosteric enzymes |
|
|
Term
|
Definition
effects of substrates on allosteric enzymes |
|
|
Term
|
Definition
the binding of substrate to one site of the allosteric enzyme influencing substrate binding to the neighboring sites without necessarily inducing a transition encompassing the entire enzyme |
|
|
Term
depiction of sequential model |
|
Definition
|
|
Term
|
Definition
the binding of one substrate decreasing the affinity of other sites on an allosteric enzyme for the substrate |
|
|
Term
the model many allosteric enzymes follow |
|
Definition
some combination of the concerted and sequential model |
|
|