Aminopeptidase By:emma dawdy

What is an enzyme and how is it created?

Enzymes are made from amino acids, and they are also proteins. An enzyme is stringed together between 100 and 1,000 amino acids in a specific order. The amino acids eventually mold into a shape. The shape allows the enzyme to carry out chemical reactions. By doing this, the enzyme speeds the chemical reaction up.

What amino acids are used in Aminopeptidase's creation?

Aminopeptidase is an exopeptidase that catalyzes the hydrolysis of amino acid residues from the amino terminus of polypeptide chains. It liberates amino acids from the N-terminal end of a number of proteins and polypeptides.

What are Aminopeptidase's substrates?

The enzyme showed a preference for substrates that contained arginine as the N-terminal residue, but was also capable of other residues such as lysine and leucine. Aminopeptidase also showed examples of C-terminal residue of dipeptide substrates.

What is Aminopeptidase's function?

Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein or peptide substrates. They are distributed throughout the animal and plant kingdoms. They are also found in subcellular organelles, in cytoplasm, and also membrane components.

How is Aminopeptidase used? How does enzyme activation work?

Aminopeptidase is used to break down proteins. Aminopeptidase is produced in the small intestine. Enzyme activation works by enzyme activators binding to enzymes to increase their activity.

How can enzymes be controlled?

By Competitive and Noncompetitive Inhibition. Cells use specific molecules to regulate enzymes in order to promote or inhibit certain chemical reactions.

Works Cited

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