Dipeptidase

Dipeptidase is an enzyme present in digestive juices that breaks down a number of protein digestion products (dipeptides) into their constituent amino acids. They are then absorbed in the human intestine.

Dipeptidase belongs to hydrolases - enzymes that catalyze the hydrolytic cleavage of chemical bonds using a water molecule. In particular, dipeptidase cleaves peptide bonds in dipeptides, producing free amino acids.

Dipeptidase is produced in the pancreas and secreted into the small intestine as part of pancreatic juice. It is active in the alkaline environment of the small intestine. In the stomach, the enzyme is inactive due to the acidic environment of gastric juice.

Dipeptidase plays an important role in the final stage of protein digestion. It completes the process of breaking down proteins into amino acids, begun by enzymes such as pepsin and trypsin. Thanks to dipeptidase, the resulting dipeptides are completely hydrolyzed to amino acids, which are then absorbed into the blood.

Dipeptidase - an enzyme of the hydrolase class that catalyzes the cleavage of the peptide bond between amino acids in a dipeptide. Dipeptidases are involved in digestion in most organisms, including humans. Enzymes that break down dipeptides are called dipeptidases, and enzymes that break down longer polypeptides are called peptidases.

Functions

– Cleavage of dipeptides resulting from the action of peptidases into amino acids, which can be used for protein synthesis.
– Participation in the regulation of amino acid levels in the blood.
– Function in cellular metabolism.

Dipeptidase breaks down dipeptides into amino acids.

The dipeptidirase system, involved in protein digestion, consists of several enzymes that catalyze a sequence of reactions leading to the formation of the amino acids that make up their parent protein. Each dipeptide is processed by a special set of digestive enzymes, often called dipeptiduria. The most common peptidases and their effects include:

Serial - hydrolyze internal peptide bonds, starting from the “middle” between amino acids in oligopeptides or polypeptide chains. Thiocarboxylate (Ser, Cys) Hydrolysis occurs with the help of thiocarbamic acid, which separates the bonds between the carboxyl and sulfhydryl groups of the amino acid residues that make up the peptide. They are part of dipeptidogen, hypoglycidin-endopeptides, glycine-dipeptidogen, thiocarboxalyl acetals, luteindipeptidegionas, isolevulinicarboxylate, sulfasalareanylcarboxyali Matazon, carbohydrate deaminase-2 and other enzymes with this type of activity

Decarboxylate Carbonate ions, such as those present in saliva, can be cleaved from amino acid residues and used as dipeptase enzymes. Enzymes of this type have a higher specificity than decarboxylate and include aminoxine benzidase, dephospholipatase A2, ERTides Dipeptiohydase - and process fragments of peptide chains formed during food fermentation and digestion