Enzyme inhibitors

... complex with) calcium and magnesium ions, both of which inhibit the enzyme trypsin. Cells themselves contain these metal ions and calcium and ... of maybe 1-5 mM. By adding EDTA to the media you reduce or remove these inhibitors. Secondarily, there are multiple membrane-associated proteases ...

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Classical competitive inhibitors compete with substrate for the active site. They lower activity by lowering the apparent affinity of the enzyme toward substrate. That shows up kinetically as an increase in the apparent Km.

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I read somewhere in my text that Non-Competitive Inhibitors will reduce the maximum rate of a chemical reaction without changing ... lines are followed by Competitive Inhibitors. Do they slow down or speed up enzyme activity? If not, what is it that they do?

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first of all, cholinesterase is an enzyme not a hormone. Now, about its overproduction: I don't really think it would ... simply block the nerve impulse, having similar effects to those of specific inhibitors of the nicotinic and muscarinic acetylcholine receptors.

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1) That kind of depends on the enzyme. 2) I don’t quite know how to answer the question. Lead is generally more toxic than zinc because it binds readily to sulfurs and tends to disrupt or precipitate proteins. Zinc, on the other hand, ligates ...

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