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T state predominates in the absence of substrate
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Figure 8-8 The MWC Model for Positive Cooperativity
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In the absence of substrate, there is more of the T state than the R state Substrate binds more tightly to the R state Within one enzyme molecule, the subunits are all T or all R
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This type of binding introduces exponents into the concentration of substrate terms so that you can draw a curve like the one shown in Fig 8-10 A substrate or effector that binds preferentially to the R state increases the concentration of the R state at equilibrium This can only happen if, in the absence of substrate or effector, the enzyme is predominantly in the T state If the enzyme were predominantly in the R state to begin with, it would already have increased affinity for the substrate and there would be no allosteric or cooperative effects Consequently, the MWC model cannot account for negative cooperativity (but this is rare anyway) Substrates can affect the conformation of the other active sites So can other molecules Effector molecules other than the substrate can bind to specific effector sites (different from the substrate-binding site) and shift the original T-R equilibrium (see Fig 8-9) An effector that binds preferentially to the T state decreases the already low concentration of the R state and makes it even more difficult for the substrate to bind These effectors decrease the velocity of the overall reaction and are referred to as allosteric inhibitors An example is the effect of ATP or citrate on the activity of phosphofructokinase Effectors that bind specif-
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Enzyme Kinetics
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Allosteric activators bind specifically to the R state and pull more of the enzyme into the more active R state
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Allosteric inhibitors bind specifically to the T state and make it harder for substrate to switch enzyme into the R state
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Figure 8-9
ALLOSTERIC EFFECTORS bind specifically to either the T or the R states Heterotropic (nonsubstrate) activators bind to and stabilize the R state, while heterotropic inhibitors bind preferentially to the T state
ically to the R state shift the T R equilibrium toward the more active (higher-affinity) R state Now all the sites are of the high-affinity R type, even before the first substrate binds Effectors that bind to the R state increase the activity (decrease the S05) and are known as allosteric activators An example is the effect of AMP on the velocity of the phosphofructokinase reaction (Fig 8-10) Notice that in the presence of an allosteric activator, the v versus [S] plot looks more hyperbolic and less sigmoidal consistent with shifting the enzyme to all R-type active sites The effects of substrates and effectors have been discussed with regard to how they could change the affinity of the enzyme for substrate (S05) It would have been just as appropriate to discuss changes in Vmax in a cooperative, or allosteric fashion
Basic Concepts in Biochemistry
Velocity
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Figure 8-10
[Fructose-6-Phosphate]
PHOSPHOFRUCTOKINASE shows positive cooperativity with fructose-6phosphate as the substrate ATP, an allosteric inhibitor, binds to the T state and decreases the velocity AMP, a signal for low energy, binds to the R state and increases the velocity of the reaction
SIGNAL TRANSDUCTION PATHWAYS
Signal Transduction Pathways Organization Signals Receptors Soluble Receptors Transmembrane Receptors Enzyme Coupled Receptors G-Protein Coupled Receptors Ion-Channel Coupled Receptors Second Messengers Amplifiers Integrators Inhibitors
SIGNAL TRANSDUCTION PATHWAYS
Allow the cell to sense and respond to signals in the environment Signal Receptor Transducer Effector upstream downstream Response
Basic Concepts in Biochemistry
Signal transduction pathways allow cells to respond to their environment and to change their behavior accordingly Signals are sensed by a receptor and changed in their form (transduced) so that they can exert their final effect on the cell In addition to the straightforward chain of events that may lead from a signal to a final effect, there are components of these pathways that are designed to amplify and integrate various cellular responses This leads to a bewildering array of biochemical interactions with branches leading off in all directions, feedback loops (that use the final effect to turn down the original response), and a series of inhibitors and activators that may activate multiple pathways at the same time The best approach for dealing with signal transduction pathways (as always, in my opinion) is to learn the various kinds of general pathways that exist and then try to fit new pathways onto these types There are a few general principles of signal transduction pathways that can be used to organize your approach
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