Luciferase.
A noncompetitive enzyme inhibitor works by binding to the enzyme at a site other than the active site, causing a change in the enzyme's shape. This change makes it harder for the substrate to bind to the enzyme, reducing its activity.
Amylopsin is an enzyme present in pancreatic juice that helps break down starch into maltose and dextrins during digestion. It works in conjunction with other enzymes to further digest carbohydrates into simpler forms for absorption in the small intestine.
The enzyme has an optimal point of pH at which the enzyme works best. For example a catalase enzyme works best in a pH of 7. When the pH changes it denatures the enzyme causing it to not be able to react with the substrate.
An enzyme that works best in an acidic environment would function best at a pH below 7, typically around pH 4 to 6. At this pH range, the enzyme's active site is more stable and optimal for catalyzing reactions.
enzyme works as a catalyst before and after the reaction it is preserved
Bioluminescence generally works because of bacteria dwelling within the animal's body. For example, an anglerfish's lure is bioluminescent because of a specie of bacteria residing there and taking their nutrition from the anglerfish.
main memory
Substrate
These are either a vitamin or mineral that works with an enzyme. The enzyme doesn't work without it (them).
enzyme works as a catalyst before and after the reaction it is preserved
The optimum pH for enzyme B is 7. Enzyme B works best at a neutral pH.
It depends on the enzyme that you want to test. If the enzyme uses or produces a compound that is detectable, and you know what compounds the enzyme needs to use/produce this, you can add a known amount of the substrate (the compound that is used) to the enzyme and measure the product (the compound that is produced) over time.Answers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comAnswers.comThis approach only works if there is only one enzyme that can act on the compound you are measuring.If you already have that enzyme in pure form you can make an antibody against it and do an Enzyme linked immunosorbent assay (ELISA) or a Western blot, which will give you a signal if the enzyme is present.
its called a substrate
Aminopeptidase
invalid question!
Lipase is the pancreatic enzyme that works on fats. It helps break down fats into fatty acids and glycerol, which can be absorbed by the body for energy.
A noncompetitive enzyme inhibitor works by binding to the enzyme at a site other than the active site, causing a change in the enzyme's shape. This change makes it harder for the substrate to bind to the enzyme, reducing its activity.