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Hydrolysis of dipeptides (e.g., leukotriene D 4, cystinyl-bis-glycine, some β-lactam antibiotics (e.g., carbapenem)) This membrane-bound, zinc enzyme has broad specificity. Inhibitors include bestatin and cilastatin .
A well known dipeptide is aspartame, an artificial sweetener. [1] Glycylglycine is the simplest dipeptide. Dipeptides are white solids. Many are far more water-soluble than the parent amino acids. [1] For example, the dipeptide Ala-Gln has the solubility of 586 g/L more than 10x the solubility of Gln (35 g/L).
Dipeptidases hydrolyze bound pairs of amino acids, called dipeptides. Dipeptidases are secreted onto the brush border of the villi in the small intestine, where they cleave dipeptides into their two component amino acids prior to absorption. They are also found within the enterocytes themselves, performing cytosolic digestion of absorbed ...
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Dipeptidase 1 (DPEP1), or renal dipeptidase, is a membrane-bound glycoprotein responsible for hydrolyzing dipeptides. It is found in the microsomal fraction of the porcine kidney cortex. [ 5 ] It exists as a disulfide-linked homodimer that is glygosylphosphatidylinositol (GPI)-anchored to the renal brush border of the kidney. [ 6 ]
Dipeptidase 2 (DPEP2) is a protein which in humans is encoded by the DPEP2 gene. [4]DPEP2 belongs to the membrane-bound dipeptidase (EC 3.4.13.19) family. These enzymes hydrolyze a variety of dipeptides, including leukotriene D 4, the beta-lactam ring of some antibiotics, and cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation.
The reaction with a second amino acid allows for the ring to open, later forming an acylated unsaturated dipeptide. The reaction happens in a step-wise function which allows for the amino group to be protected and the azlactone to be produced. Catalytic hydrogenation and hydrolysis then take place in order to produce the dipeptide . [6]