N-Acetylglutamine

Found 10 Sample Hits

m/z	Adducts	Species	Organ	Scanning	Sample
188.1006	[M-H2O+NH4]+ PPM:12.6	Homo sapiens	esophagus	DESI ()	LNTO22_1_3 - MTBLS385 Resolution: 75μm, 121x68 Description
188.1005	[M-H2O+NH4]+ PPM:13.1	Homo sapiens	esophagus	DESI ()	LNTO29_16_2 - MTBLS385 Resolution: 17μm, 95x101 Description
206.1167	[M+NH4]+ PPM:15.4	Homo sapiens	esophagus	DESI ()	LNTO29_16_2 - MTBLS385 Resolution: 17μm, 95x101 Description
188.1009	[M-H2O+NH4]+ PPM:11	Homo sapiens	esophagus	DESI ()	LNTO22_1_9 - MTBLS385 Resolution: 75μm, 89x74 Description
188.1004	[M-H2O+NH4]+ PPM:13.6	Homo sapiens	esophagus	DESI ()	LNTO29_16_3 - MTBLS385 Resolution: 17μm, 108x107 Description
206.1163	[M+NH4]+ PPM:13.4	Homo sapiens	esophagus	DESI ()	LNTO29_16_3 - MTBLS385 Resolution: 17μm, 108x107 Description
188.1006	[M-H2O+NH4]+ PPM:12.6	Homo sapiens	esophagus	DESI ()	LNTO22_1_8 - MTBLS385 Resolution: 75μm, 69x61 Description
188.1006	[M-H2O+NH4]+ PPM:12.6	Homo sapiens	esophagus	DESI ()	LNTO22_2_1 - MTBLS385 Resolution: 75μm, 89x88 Description
188.1012	[M-H2O+NH4]+ PPM:9.4	Homo sapiens	esophagus	DESI ()	LNTO22_2_2 - MTBLS385 Resolution: 75μm, 135x94 Description
206.1164	[M+NH4]+ PPM:13.9	Homo sapiens	esophagus	DESI ()	LNTO29_18_2 - MTBLS385 Resolution: 75μm, 62x68 Description

N-Acetyl-L-glutamine (NAcGln) or N-Acetylglutamine, belongs to the class of organic compounds known as N-acyl-alpha amino acids. N-acyl-alpha amino acids are compounds containing an alpha amino acid which bears an acyl group at its terminal nitrogen atom. N-Acetylglutamine can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetylglutamine is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-glutamine. N-acetyl amino acids can be produced either via direct synthesis of specific N-acetyltransferases or via the proteolytic degradation of N-acetylated proteins by specific hydrolases. N-terminal acetylation of proteins is a widespread and highly conserved process in eukaryotes that is involved in protection and stability of proteins (PMID: 16465618). About 85\\\% of all human proteins and 68\\\% of all yeast proteins are acetylated at their N-terminus (PMID: 21750686). Several proteins from prokaryotes and archaea are also modified by N-terminal acetylation. The majority of eukaryotic N-terminal-acetylation reactions occur through N-acetyltransferase enzymes or NAT‚Äôs (PMID: 30054468). These enzymes consist of three main oligomeric complexes NatA, NatB, and NatC, which are composed of at least a unique catalytic subunit and one unique ribosomal anchor. The substrate specificities of different NAT enzymes are mainly determined by the identities of the first two N-terminal residues of the target protein. The human NatA complex co-translationally acetylates N-termini that bear a small amino acid (A, S, T, C, and occasionally V and G) (PMID: 30054468). NatA also exists in a monomeric state and can post-translationally acetylate acidic N-termini residues (D-, E-). NatB and NatC acetylate N-terminal methionine with further specificity determined by the identity of the second amino acid. N-acetylated amino acids, such as N-acetylglutamine can be released by an N-acylpeptide hydrolase from peptides generated by proteolytic degradation (PMID: 16465618). In addition to the NAT enzymes and protein-based acetylation, N-acetylation of free glutamine can also occur. In particular, N-Acetylglutamine can be biosynthesized from L-glutamine and acetyl-CoA by the enzyme glutamine N-acyltransferase (EC 2.3.1.68). Excessive amounts N-acetyl amino acids including N-acetylglutamine (as well as N-acetylglycine, N-acetylserine, N-acetylmethionine, N-acetylglutamate, N-acetylalanine, N-acetylleucine and smaller amounts of N-acetylthreonine, N-acetylisoleucine, and N-acetylvaline) can be detected in the urine with individuals with acylase I deficiency, a genetic disorder (PMID: 16465618). Aminoacylase I is a soluble homodimeric zinc binding enzyme that catalyzes the formation of free aliphatic amino acids from N-acetylated precursors. In humans, Aminoacylase I is encoded by the aminoacylase 1 gene (ACY1) on chromosome 3p21 that consists of 15 exons (OMIM 609924). Individuals with aminoacylase I deficiency will experience convulsions, hearing loss and difficulty feeding (PMID: 16465618). ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. Many N-acetylamino acids, including N-acetylglutamine are classified as uremic toxins if present in high abundance in the serum or plasma (PMID: 26317986; PMID: 20613759). Uremic toxins are a diverse group of endogenously produced molecules that, if not properly cleared or eliminated by the kidneys, can cause kidney damage, cardiovascular disease and neurological deficits (PMID: 18287557). N-acetylglutamine can be used for parenteral nutrition as a source of glutamine since glutamine is too unstable whereas N-acetylglutamine is very stable. In patients treated with aminoglycosides and/or glycopeptides, an elevation of N-acetylglutamine in urine suggests renal tubular injury. N-Acetylglutamine (GIcNAc) is a modified amino acid (an acetylated analogue of glutamine), a metabolite present in normal human urine. The decomposition products of GIcNAc have been identified by NMR and HPLC-MS as N-acetyl-L-glutamic acid, N-(2,6-dioxo-3-piperidinyl) acetamide, pyroglutamic acid, glutamic acid, and glutamine. GIcNAc is used for parenteral nutrition as a source of glutamine, since glutamine is too unstable, but GIcNAc is very stable. In patients treated with aminoglycosides and/or glycopeptides, elevation GIcNAc in urine suggests renal tubular injury. High amounts of N-acetylated amino acids (i.e.: N-Acetylglutamine) were detected patient with aminoacylase I deficiency (EC 3.5.1.14, a homodimeric zinc-binding metalloenzyme located in the cytosol), a novel inborn error of metabolism. (PMID: 15331932, 11312773, 7952062, 2569664, 16274666) [HMDB] C78272 - Agent Affecting Nervous System > C47795 - CNS Stimulant Aceglutamide (α-N-Acetyl-L-glutamine) is a psychostimulant and nootropic, used to improve memory and concentration[1].