Exact Mass: 218.0903
Exact Mass Matches: 218.0903
Found 37 metabolites which its exact mass value is equals to given mass value 218.0903,
within given mass tolerance error 0.001 dalton. Try search metabolite list with more accurate mass tolerance error
0.0002 dalton.
Alanylglutamic acid
Alanylglutamic acid is a dipeptide composed of alanine and glutamic acid. It is an incomplete breakdown product of protein digestion or protein catabolism. Some dipeptides are known to have physiological or cell-signaling effects although most are simply short-lived intermediates on their way to specific amino acid degradation pathways following further proteolysis. Ala-Glu-OH is an agent of the dipeptide[1][2].
gamma-Glutamylalanine
gamma-Glutamylalanine is a dipeptide composed of gamma-glutamate and alanine, and is a proteolytic breakdown product of larger proteins. It belongs to the family of N-acyl-alpha amino acids and derivatives. These are compounds containing an alpha amino acid which bears an acyl group at its terminal nitrogen atom. gamma-Glutamylalanine is a natural substrate of the enzyme (5-L-glutamyl)-L-amino acid 5-glutamyltransferase (cyclizing) (g-glutamylcyclotransferase, EC 2.3.2.2) in the glutathione metabolism pathway, which cleaves gamma-glutamylalanine to produce L-5-oxoproline. gamma-Glutamylcyclotransferase is widely distributed in both human and animal tissues where it catalyzes the scission of the y-peptide bonds of many different gamma-glutamyl-amino acids and gamma-glutamyl-gamma-glutamyl-amino acids. The latter are better substrates of the enzyme than the corresponding gamma-glutamyl-amino acids (PMID: 2570694, 2893631). 5-L-Glutamyl-L-alanine is a natural substrate of the enzyme 5-L-glutamyl)-L-amino acid 5-glutamyltransferase (cyclizing) (g-glutamylcyclotransferase, EC 2.3.2.2) in the glutathione metabolism pathway, which cleaves 5-L-Glutamyl-L-alanine, producing L-5-oxoproline. gamma-Glutamylcyclotransferase is widely distributed in both human and animal tissues where it catalyzes the scission of the y-peptide bonds of many different gamma-glutamyl-aminoacids and gamma-glutamyl-gamma-glutamyl-amino-acids. The latter are better substrates of the enzyme than the corresponding gamma-glutamyl - amino-acids. (PMID: 2570694, 2893631) [HMDB]
Glutamylalanine
Glutamylalanine is a naturally occurring dipeptide, composed of glutamate and alanine. Glutamylalanine is essential in the supply of glutamate to human erythrocytes. Human erythrocytes are essentially impermeable to glutamate and yet there is a continual requirement for the amino acid for glutathione synthesis. In addition, the intracellular glutamate concentration is approximately five times that of plasma. Glutamylalanine enters the human erythrocyte through saturable membrane-transport systems describable by Michaelis-Menten kinetics. The cytosolic red cell peptidases have a vast capacity to hydrolyse the dipeptide in a process also describable by simple Michaelis-Menten kinetics. The transport process is the rate-determining step in the pathway leading to the production of intracellular glutamate from extracellular glutamylalanine. Glutamylalanine is transported by the human oligopeptide transporter, hPepT1, situated in the small intestine, which is involved in the absorption of nutrient oligopeptides and transports numerous di- and tripeptides. This active transport is being tested for use as a strategy to increase the permeability across the intestine for larger biologically active molecules with low intestinal permeability, in a therapeutic attempt to transport dipeptide-coupled active drug substances via hPepT1 (PMID: 2860897, 11557350).
Hydroxyprolyl-Serine
Hydroxyprolyl-Serine is a dipeptide composed of hydroxyproline and serine. It is an incomplete breakdown product of protein digestion or protein catabolism. Some dipeptides are known to have physiological or cell-signaling effects although most are simply short-lived intermediates on their way to specific amino acid degradation pathways following further proteolysis. This dipeptide has not yet been identified in human tissues or biofluids and so it is classified as an Expected metabolite.
Serylhydroxyproline
Serylhydroxyproline is a dipeptide composed of serine and hydroxyproline. It is an incomplete breakdown product of protein digestion or protein catabolism. Dipeptides are organic compounds containing a sequence of exactly two alpha-amino acids joined by a peptide bond. Some dipeptides are known to have physiological or cell-signalling effects although most are simply short-lived intermediates on their way to specific amino acid degradation pathways following further proteolysis.
N-gamma-L-Glutamyl-D-alanine
N-gamma-L-Glutamyl-D-alanine is found in pulses. N-gamma-L-Glutamyl-D-alanine is isolated from young pea shoots Pisum sativu Isolated from young pea shoots Pisum sativum. N-gamma-L-Glutamyl-D-alanine is found in pulses and common pea.
heliopine|N2-(1R-carboxyethyl)-L-glutamine|vitopine
Glutamylalanine
Glutamylalanine is a naturally occurring dipeptide. Glutamylalanine is essential in the supply of glutamate to human erythrocytes. Human erythrocytes are essentially impermeable to glutamate and yet there is a continual requirement for the amino acid for glutathione synthesis. In addition, the intracellular glutamate concentration is approximately five times that of plasma. Glutamylalanine enters the human erythrocyte through saturable membrane-transport systems describable by Michaelis- Menten kinetics. The cytosolic red cell peptidases have a vast capacity to hydrolyse the dipeptide in a process also describable by simple Michaelis-Menten kinetics. The transport process is the rate-determining step in the pathway leading to the production of intracellular glutamate from extracellular glutamylalanine. Glutamylalanine is transported by the human oligopeptide transporter, hPepT1, situated in the small intestine, which is involved in the absorption of nutrient oligopeptides and transports numerous di- and tripeptides. This active transport is being tested for use as a strategy to increase the permeability across the intestine for larger biologically active molecules with low intestinal permeability, in a therapeutic attempt to transport dipeptide-coupled active drug substances via hPepT1. (PMID: 2860897, 11557350) [HMDB]
2-Amino-5-[(1-carboxyethyl)amino]-5-oxopentanoic acid
1-(2-amino-3-hydroxypropanoyl)-4-hydroxypyrrolidine-2-carboxylic acid
gamma-Glu-Ala
A gamma-glutamylalanine obtained by formal condensation of the gamma-carboxy group of L-glutamic acid with the amino group of L-alanine.
