What can cause enzymes to become inhibited?

Question

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Answer 1

1.Tempeartute:enzyme activity is high at temp 30-40C.Inactivation sets in and is complete above 50-55C

2.pH:At extreme acidity or alkalinity the denaturaturation of protein takes place with loss of enzyme activity(most enzymes are active at pH range of 4.5 to 8.0)

3.Electrilytes:it varies from enzyme to enzyme ,a given ion may be activator for one but an inhibtor for another.
(enzyme concentration and substrate concentration) proportional to enzyme activity)

Enzymes can be regulated by inhibitors.

Enzyme inhibitors are molecules that bind to enzymes and decrease their activity.The binding of an inhibitor can stop a substrate from entering the enzyme's active site and/or hinder the enzyme from catalysing its reaction

Enzyme inhibitors also occur naturally and are involved in the regulation of metabolism. For example, enzymes in a metabolic pathway can be inhibited by downstream products. This type of negative feedback slows flux through a pathway when the products begin to build up and is an important way to maintain homeostasis in a cell

Other cellular enzyme inhibitors are proteins that specifically bind to and inhibit an enzyme target. This can help control enzymes that may be damaging to a cell, such as proteases or nucleases; a well-characterised example is the ribonuclease inhibitor, which binds to ribonucleases in one of the tightest known protein–protein interactions

Natural enzyme inhibitors can also be poisons and are used as defenses against predators or as ways of killing prey.