Chemical Formula: C7H12N2O4

Chemical Formula C7H12N2O4

Found 41 metabolite its formula value is C7H12N2O4

Tabtoxinine-delta-lactam

C7H12N2O4 (188.07970319999998)

A delta-lactam that is L-pipecolic acid carrying additional hydroxy and aminomethyl substituents at position 5 as well as an oxo substituent at position 6.

N-Acetylglutamine

(2S)-2-Acetamido-5-amino-5-oxopentanoic acid

C7H12N2O4 (188.07970319999998)

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].

Glycylhydroxyproline

(2S,4R)-1-(2-aminoacetyl)-4-hydroxypyrrolidine-2-carboxylic acid

C7H12N2O4 (188.07970319999998)

Glycylhydroxyproline is likely a proteolytic breakdown product of collagen. It belongs to the family of peptides. These are compounds containing an amide derived from two or more amino carboxylic acid molecules (the same or different) by the formation of a covalent bond from the carbonyl carbon of one to the nitrogen atom of another. It is found in urine (PMID: 3782411). A dipeptide found in urine (PMID: 3782411). This is a proteolytic breakdown product of collagen. [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].