Exact Mass: 407.2519
Exact Mass Matches: 407.2519
Found 91 metabolites which its exact mass value is equals to given mass value 407.2519,
within given mass tolerance error 0.01 dalton. Try search metabolite list with more accurate mass tolerance error
0.001 dalton.
Leu-Leu-Tyr
Acquisition and generation of the data is financially supported in part by CREST/JST. KEIO_ID L007
Geranylgeranylcysteine
Geranylgeranylcysteine is a modified thioether amino acid in which an isoprenyl group (geranylgeranyl) has been attached to the sulfhydryl group of cysteine through a thioether bond. Geranylgeranylcysteine is typically formed through posttranslational (prenylation) protein modification whereupon degradation of the parent protein leaves the modified (prenylated) amino acid. Prenylation is a relatively recently discovered post-translational modification of proteins that directs cytosollic proteins to membranes while at the same time activating them functionally. The change in hydrophobicity that is essential for membrane binding is done via the covalent attachment of a polyisoprene (such as a farnesyl or geranylgeranyl group) to a C-terminal cysteine by a thioether bond. Prenylated proteins can comprise up to 2\\% of total cellular protein. Prenylcysteine lyase is an enzyme that is capable of cleaving the thiother bond in prenylcysteines and is used to help in the turnover of prenylated proteins. Prenylcysteine lyase deficiency leads to the accumulation of farnesylcysteine and geranylgeranylcysteine in brain and liver. (PMID: 9287348) [HMDB] Geranylgeranylcysteine is a modified thioether amino acid in which an isoprenyl group (geranylgeranyl) has been attached to the sulfhydryl group of cysteine through a thioether bond. Geranylgeranylcysteine is typically formed through posttranslational (prenylation) protein modification whereupon degradation of the parent protein leaves the modified (prenylated) amino acid. Prenylation is a relatively recently discovered post-translational modification of proteins that directs cytosollic proteins to membranes while at the same time activating them functionally. The change in hydrophobicity that is essential for membrane binding is done via the covalent attachment of a polyisoprene (such as a farnesyl or geranylgeranyl group) to a C-terminal cysteine by a thioether bond. Prenylated proteins can comprise up to 2\\% of total cellular protein. Prenylcysteine lyase is an enzyme that is capable of cleaving the thiother bond in prenylcysteines and is used to help in the turnover of prenylated proteins. Prenylcysteine lyase deficiency leads to the accumulation of farnesylcysteine and geranylgeranylcysteine in brain and liver. (PMID: 9287348).
Neurotensin 11-13
Neurotensin is a 13 amino acid neuropeptide that is implicated in the regulation of luteinizing hormone and prolactin release and has significant interaction with the dopaminergic system. Neurotensin was first isolated from extracts of bovine hypothalamus based on its ability to cause a visible vasodilation in the exposed cutaneous regions of anesthetized rats. This structure shows the 11-13 fragment of neurotensin. Neurotensin is a 13 amino acid neuropeptide that is implicated in the regulation of luteinizing hormone and prolactin release and has significant interaction with the dopaminergic system. Neurotensin was first isolated from extracts of bovine hypothalamus based on its ability to cause a visible vasodilation in the exposed cutaneous regions of anesthetized rats
N-Arachidonoyl Cysteine
N-arachidonoyl cysteine belongs to the class of compounds known as N-acylamides. These are molecules characterized by a fatty acyl group linked to a primary amine by an amide bond. More specifically, it is an Arachidonic acid amide of Cysteine. It is believed that there are more than 800 types of N-acylamides in the human body. N-acylamides fall into several categories: amino acid conjugates (e.g., those acyl amides conjugated with amino acids), neurotransmitter conjugates (e.g., those acylamides conjugated with neurotransmitters), ethanolamine conjugates (e.g., those acylamides conjugated to ethanolamine), and taurine conjugates (e.g., those acyamides conjugated to taurine). N-Arachidonoyl Cysteine is an amino acid conjugate. N-acylamides can be classified into 9 different categories depending on the size of their acyl-group: 1) short-chain N-acylamides; 2) medium-chain N-acylamides; 3) long-chain N-acylamides; and 4) very long-chain N-acylamides; 5) hydroxy N-acylamides; 6) branched chain N-acylamides; 7) unsaturated N-acylamides; 8) dicarboxylic N-acylamides and 9) miscellaneous N-acylamides. N-Arachidonoyl Cysteine is therefore classified as a long chain N-acylamide. N-acyl amides have a variety of signaling functions in physiology, including in cardiovascular activity, metabolic homeostasis, memory, cognition, pain, motor control and others (PMID: 15655504). N-acyl amides have also been shown to play a role in cell migration, inflammation and certain pathological conditions such as diabetes, cancer, neurodegenerative disease, and obesity (PMID: 23144998; PMID: 25136293; PMID: 28854168).N-acyl amides can be synthesized both endogenously and by gut microbiota (PMID: 28854168). N-acylamides can be biosynthesized via different routes, depending on the parent amine group. N-acyl ethanolamines (NAEs) are formed via the hydrolysis of an unusual phospholipid precursor, N-acyl-phosphatidylethanolamine (NAPE), by a specific phospholipase D. N-acyl amino acids are synthesized via a circulating peptidase M20 domain containing 1 (PM20D1), which can catalyze the bidirectional the condensation and hydrolysis of a variety of N-acyl amino acids. The degradation of N-acylamides is largely mediated by an enzyme called fatty acid amide hydrolase (FAAH), which catalyzes the hydrolysis of N-acylamides into fatty acids and the biogenic amines. Many N-acylamides are involved in lipid signaling system through interactions with transient receptor potential channels (TRP). TRP channel proteins interact with N-acyl amides such as N-arachidonoyl ethanolamide (Anandamide), N-arachidonoyl dopamine and others in an opportunistic fashion (PMID: 23178153). This signaling system has been shown to play a role in the physiological processes involved in inflammation (PMID: 25136293). Other N-acyl amides, including N-oleoyl-glutamine, have also been characterized as TRP channel antagonists (PMID: 29967167). N-acylamides have also been shown to have G-protein-coupled receptors (GPCRs) binding activity (PMID: 28854168). The study of N-acylamides is an active area of research and it is likely that many novel N-acylamides will be discovered in the coming years. It is also likely that many novel roles in health and disease will be uncovered for these molecules.
5,13-dihydroxy-2,4,6,14-tetramethyl-15-(2-methyl-1,3-thiazol-4-yl)pentadeca-10,14-dien-3-one
3-(4,6-dipyrrolidin-1-yl-1,3,5-triazin-2-yl)-1,2,3,4,5,6-hexahydro-8H-1,5-methanopyrido[1,2-a][1,5]diazocin-8-one, 11-(4,6-dipyrrolidinyl-1,3,5-triazin-2-yl)-7,11-diazatricyclo[7.3.1.0<2,7>]tri deca-2,4-dien-6-one
relative retention time with respect to 9-anthracene Carboxylic Acid is 0.968 relative retention time with respect to 9-anthracene Carboxylic Acid is 0.973
