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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).
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]
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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An exopeptidase is any peptidase that catalyzes the cleavage of the terminal (or the penultimate) peptide bond; the process releases a single amino acid, dipeptide or a tripeptide from the peptide chain. [1]
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.
Transcription occurs in the nucleus using DNA as a template to produce mRNA.In eukaryotes, this mRNA molecule is known as pre-mRNA as it undergoes post-transcriptional modifications in the nucleus to produce a mature mRNA molecule.