Exact Mass: 555.2692852
Exact Mass Matches: 555.2692852
Found 92 metabolites which its exact mass value is equals to given mass value 555.2692852,
within given mass tolerance error 8.0E-6 dalton. Try search metabolite list with more accurate mass tolerance error
1.6E-6 dalton.
Enkephalin L
Enkephalin L is an opioid peptide. Opioid peptides are a group of neuropeptides which include enkephalins, endorphins and dynorphins. In addition to their central and peripheral antinociceptive function, opioids can modulate immune activity and cell proliferation. Enkephalins typically have a turnover rate measured in seconds to minutes, both in vivo and in vitro, and this stability is related to the age of the cell system under study. It is noteworthy that the residues most essential to enkephalin function are also either neurotransmitters themselves (glycine) or immediate precursors of L-Dopa, dopamine and norepinephrine (tyrosine and phenylalanine). The variable fifth amino acid leucine (leu5) or methionine (met5) has not yet been assigned any neurotransmitter candidacy. Again, this suggests that enkephalin is polyfunctional in that, in its intact state it elicits binding to the same sites in the brain as morphine and other opiates, and its degradation products have a potential for follow-up accessory functions by reacting as signaling entities themselves, or as the immediate precursors to inhibitory or metabotropic neurotransmitters. Enkephalins are present in macrophages infiltrating the dermal papillae in involved psoriatic skin and that the amount of enkephalin is significantly increased in involved psoriatic skin. Major enkephalin pathways in the brain involve the extrapyramidal system, including motor pathways controlled by the basal ganglia, the limbic system that governs emotional and behavioral control, and the hypothalamic-neuroendocrine axis. The apparent overlap of localization within the central nervous system of dopaminergic, glycinergic, and enkephalinergic pathways is speculated to be of neurophysiological significance, especially in light of the relatively short half-life of the enkephalins and the immediate precursor-product relationship between tyrosine and dopamine, and glycinergic signaling. Enkephalins are released into the bloodstream of mammals by the adrenal medulla. Once they are in the blood, these peptides undergo a fairly rapid hydrolysis by several plasma-contained enzymes. However, a fraction of the enkephalins present in the plasma are bound to the serum albumin, and the bound peptides are almost completely intact even after a long incubation in the presence of serum enzymes. (PMID: 9450624, 16802191, 4069309) [HMDB] Enkephalin L is an opioid peptide. Opioid peptides are a group of neuropeptides which include enkephalins, endorphins and dynorphins. In addition to their central and peripheral antinociceptive function, opioids can modulate immune activity and cell proliferation. Enkephalins typically have a turnover rate measured in seconds to minutes, both in vivo and in vitro, and this stability is related to the age of the cell system under study. It is noteworthy that the residues most essential to enkephalin function are also either neurotransmitters themselves (glycine) or immediate precursors of L-Dopa, dopamine and norepinephrine (tyrosine and phenylalanine). The variable fifth amino acid leucine (leu5) or methionine (met5) has not yet been assigned any neurotransmitter candidacy. Again, this suggests that enkephalin is polyfunctional in that, in its intact state it elicits binding to the same sites in the brain as morphine and other opiates, and its degradation products have a potential for follow-up accessory functions by reacting as signaling entities themselves, or as the immediate precursors to inhibitory or metabotropic neurotransmitters. Enkephalins are present in macrophages infiltrating the dermal papillae in involved psoriatic skin and that the amount of enkephalin is significantly increased in involved psoriatic skin. Major enkephalin pathways in the brain involve the extrapyramidal system, including motor pathways controlled by the basal ganglia, the limbic system that governs emotional and behavioral control, and the hypothalamic-neuroendocrine axis. The apparent overlap of localization within the central nervous system of dopaminergic, glycinergic, and enkephalinergic pathways is speculated to be of neurophysiological significance, especially in light of the relatively short half-life of the enkephalins and the immediate precursor-product relationship between tyrosine and dopamine, and glycinergic signaling. Enkephalins are released into the bloodstream of mammals by the adrenal medulla. Once they are in the blood, these peptides undergo a fairly rapid hydrolysis by several plasma-contained enzymes. However, a fraction of the enkephalins present in the plasma are bound to the serum albumin, and the bound peptides are almost completely intact even after a long incubation in the presence of serum enzymes. (PMID: 9450624, 16802191, 4069309). D018377 - Neurotransmitter Agents > D018847 - Opioid Peptides D018377 - Neurotransmitter Agents > D004745 - Enkephalins [Leu5]-Enkephalin is a pentapeptide with morphine like properties. [Leu5]-Enkephalin is a five amino acid endogenous peptide that acts as an agonist at opioid receptors. [Leu5]-Enkephalin is a pentapeptide with morphine like properties. [Leu5]-Enkephalin is a five amino acid endogenous peptide that acts as an agonist at opioid receptors. [Leu5]-Enkephalin is a pentapeptide with morphine like properties. [Leu5]-Enkephalin is a five amino acid endogenous peptide that acts as an agonist at opioid receptors.
YGGFL
D018377 - Neurotransmitter Agents > D018847 - Opioid Peptides D018377 - Neurotransmitter Agents > D004745 - Enkephalins
Asp Phe Phe Lys
Asp Phe Lys Phe
Asp Lys Phe Phe
Phe Asp Phe Lys
Phe Asp Lys Phe
Phe Phe Asp Lys
Phe Phe Lys Asp
Phe Ile Asn Tyr
Phe Ile Tyr Asn
Phe Lys Asp Phe
Phe Lys Phe Asp
Phe Leu Asn Tyr
Phe Leu Tyr Asn
Phe Asn Ile Tyr
Phe Asn Leu Tyr
Phe Asn Tyr Ile
Phe Asn Tyr Leu
Phe Gln Val Tyr
Phe Gln Tyr Val
Phe Val Gln Tyr
Phe Val Tyr Gln
Phe Tyr Ile Asn
Phe Tyr Leu Asn
Phe Tyr Asn Ile
Phe Tyr Asn Leu
Phe Tyr Gln Val
Phe Tyr Val Gln
Ile Phe Asn Tyr
Ile Phe Tyr Asn
Ile Asn Phe Tyr
Ile Asn Tyr Phe
Ile Tyr Phe Asn
Ile Tyr Asn Phe
Lys Asp Phe Phe
Lys Phe Asp Phe
Lys Phe Phe Asp
Leu Phe Asn Tyr
Leu Phe Tyr Asn
Leu Asn Phe Tyr
Leu Asn Tyr Phe
Leu Tyr Phe Asn
Leu Tyr Asn Phe
Asn Phe Ile Tyr
Asn Phe Leu Tyr
Asn Phe Tyr Ile
Asn Phe Tyr Leu
Asn Ile Phe Tyr
Asn Ile Tyr Phe
Asn Leu Phe Tyr
Asn Leu Tyr Phe
Asn Tyr Phe Ile
Asn Tyr Phe Leu
Asn Tyr Ile Phe
Asn Tyr Leu Phe
Gln Phe Val Tyr
Gln Phe Tyr Val
Gln Val Phe Tyr
Gln Val Tyr Phe
Gln Tyr Phe Val
Gln Tyr Val Phe
Val Phe Gln Tyr
Val Phe Tyr Gln
Val Gln Phe Tyr
Val Gln Tyr Phe
Val Tyr Phe Gln
Val Tyr Gln Phe
Tyr Phe Ile Asn
Tyr Phe Leu Asn
Tyr Phe Asn Ile
Tyr Phe Asn Leu
Tyr Phe Gln Val
Tyr Phe Val Gln
Tyr Ile Phe Asn
Tyr Ile Asn Phe
Tyr Leu Phe Asn
Tyr Leu Asn Phe
Tyr Asn Phe Ile
Tyr Asn Phe Leu
Tyr Asn Ile Phe
Tyr Asn Leu Phe
Tyr Gln Phe Val
Tyr Gln Val Phe
Tyr Val Phe Gln
Tyr Val Gln Phe
Leu-Enkephalin
A pentapeptide comprising L-tyrosine, glycine, glycine, L-phenylalanine and L-leucine residues joined in sequence by peptide linkages. It is an endogenous opioid peptide produced in vertebrate species, including rodents, primates and humans that results from decomposition of proenkephalin or dynorphin and exhibits antinociceptive properties.
Leu-enkephalin zwitterion
A peptide zwitterion obtained by transfer of a proton from the carboxy to the amino terminus of Leu-enkephalin. Major species at pH 7.3.