I would say residential possibly
PDK1 (pyruvate dehydrogenase kinase 1) is an enzyme which inactivates the pyruvate dehydrogenase by phosphorylating it using an ATP molecule<span>.
</span><span>PDK1 (phosphoinositide-dependent protein kinase-1) acts by catalyzing the phosphorylation of Thr-229 (threonine at position 229 in pyruvate dehydrogenase).
This phosphorylation is </span><span>synergistic</span> with the phosphorylation of C-terminal Thr-389, but this one is not done by the PDK1.
All of these industries would be the correct answer
Answer:
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Explanation:
I would like brainiest please.
Answer:
Explanation:
An allosteric enzyme is one in which the activity of the enzyme can be controlled by the biniding of a molecule to the "allosteric site". This really just means somewhere other than the active site. Thus allosteric control of an enzyme can be classed in two ways. A positive allosteric modification is the binding of a molecule to the enzyme which increase the rate of reaction. Sort of like catalysing the catalysing effect of an enzyme. Obviously the opposite is true of negative allosteric modification. A good example for this is the activity of phosphofructokinase, which is promoted by a high AMP concentration, and inhibited by a high ATP concentration. This should make sense if you think about the action of a kinase etc.
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