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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 ...
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 .
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]
Glycylglycine is the dipeptide of glycine, making it the simplest peptide. [1] The compound was first synthesized by Emil Fischer and Ernest Fourneau in 1901 by boiling 2,5-diketopiperazine (glycine anhydride) with hydrochloric acid. [2] Shaking with alkali [1] and other synthesis methods have been reported. [3]
A dipeptide has two amino acids. A tripeptide has three amino acids. A tetrapeptide has four amino acids. A pentapeptide has five amino acids. (e.g., enkephalin). A hexapeptide has six amino acids. (e.g., angiotensin IV). A heptapeptide has seven amino acids. (e.g., spinorphin). An octapeptide has eight amino acids (e.g., angiotensin II).
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.
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