Competitive inhibition vs allosteric inhibition
In competitive the substrate and inhibitor bind at the same active site - pretty straightforward. In allosteric regulation (speaking specifically about inhibition here), the inhibitor is binding at a site other than the active site, and changing the enzyme in some way to make it inactive.
Answer:
Trypsin cuts at lysine and arginine amino acid residues at the carboxyl end. Chymotrypsin cuts at tryosine , phenylalanine, and tryptophan amino acid residues at the carboxyl end.
Explanation:
Trypsin and chymotrypsin are known as proteolytic enzymes which are actively involved in the digestive system. They are both secreted by the pancreas and are majorly involved in the breakdown of protein in the small intestine.
Trypsin cuts at lysine and arginine amino acid residues at the carboxyl end. Chymotrypsin cuts at tryosine , phenylalanine, and tryptophan amino acid residues at the carboxyl end.
Answer: A
Explanation:
it’s a hands free device that prevents water being wasted
True that should be the answer
Answer:
because of inefficiency
Explanation:
The organisms that eat the primary consumers are meat eaters (carnivores) and are called the secondary consumers. ... Because of this inefficiency, there is only enough food for a few top level consumers, but there is lots of food for herbivores lower down on the food chain. There are fewer consumers than producers.
