As these cellular demands and conditions changes, so do the amounts and functionality of different enzymes.
factors that can affect or control enzyme activity. These include pH and temperature (discussed in the active site article), as well as:
Enzyme activity may be turned "up" or "down" by activator and inhibitor molecules that bind specifically to the enzyme.
Many enzymes are only active when bound to non-protein helper molecules known as cofactors.
Storing enzymes in specific compartments can keep them from doing damage or provide the right conditions for activity.
Key metabolic enzymes are often inhibited by the end product of the pathway they control (feedback inhibition).
an activator or inhibitor's binding is reversible,
reversible inhibitor. 1 1
It blocks activity of a viral enzyme that helps the virus make more copies of itself
That is, only the inhibitor or the substrate can be bound at a given moment.
Instead, it attaches at another site and blocks the enzyme from doing its job.
it will decrease reaction rate when there's not much substrate, but can be "out-competed" by lots of substrate
binds to an enzyme someplace other than the active site
allosterically regulated have a set of unique properties that set them apart
Allosteric enzymes typically have multiple active sites located on different protein subunits.
Also, in a process called cooperativity, the substrate itself can serve as an allosteric activator: when it binds to one active site, the activity of the other active sites goes up. 3 3 cubed This is considered allosteric regulation because the substrate affects active sites far from its binding site.
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