Exact Mass: 174.0632
Exact Mass Matches: 174.0632
Found 35 metabolites which its exact mass value is equals to given mass value 174.0632,
within given mass tolerance error 0.001 dalton. Try search metabolite list with more accurate mass tolerance error
0.0002 dalton.
Formiminoglutamic acid
Measurement of this acid in the urine after oral administration of histidine provides the basis for the diagnostic test of folic acid deficiency and of megaloblastic anemia of pregnancy. [HMDB] Measurement of this acid in the urine after oral administration of histidine provides the basis for the diagnostic test of folic acid deficiency and of megaloblastic anemia of pregnancy.
N-Acetylasparagine
N-Acetyl-L-asparagine or N-Acetylasparagine, 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-Acetylasparagine can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetylasparagine is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-asparagine. 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’s (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-acetylasparagine 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 asparagine can also occur. In particular, N-Acetylasparagine can be biosynthesized from L-asparagine and acetyl-CoA by the enzyme NAT1 or the arylamine acetyltransferase I (https://doi.org/10.1096/fasebj.31.1_supplement.821.8). Many N-acetylamino acids 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). A human metabolite taken as a putative food compound of mammalian origin [HMDB] (S)-2-acetamido-4-amino-4-oxobutanoic acid is an endogenous metabolite.
Na-Acetyl-L-asparagine
(S)-2-acetamido-4-amino-4-oxobutanoic acid is an endogenous metabolite.
N-Acetylasparagine
(S)-2-acetamido-4-amino-4-oxobutanoic acid is an endogenous metabolite.
Furo[2,3-d]oxazole-5-methanol,2-amino-3a,5,6,6a-tetrahydro-6-hydroxy-, (3aR,5R,6R,6aS)-
Formiminoglutamic acid
The N-formimidoyl derivative of L-glutamic acid
