Exact Mass: 160.12117160000003

Exact Mass Matches: 160.12117160000003

Found 45 metabolites which its exact mass value is equals to given mass value 160.12117160000003, within given mass tolerance error 0.0002 dalton. Try search metabolite list with more accurate mass tolerance error 4.0E-5 dalton.

N(6)-Methyllysine

epsilon-N-Methyllysine hydrochloride, (L-lys)-isomer

C7H16N2O2 (160.12117160000003)

N(6)-Methyllysine is a naturally occurring amino acid found in human biofluids. N-monomethyl-lysine is generated by metabolic transmethylation of endogenous lysine. Lysine methylation displays the highest degree of complexity among known covalent histone modifications, with each site of methylation regulating the association of different effector molecules. The versatility of lysine methylation marks is perhaps best exemplified by modifications implicated in transcriptional regulation as well as being required for double-strand break repair in several organisms. Identification of the numerous biological functions encoded by histone lysine methylation is a major area of research interest, as these mechanisms are intimately associated with cellular senescence, genomic instability, and leukemogenesis. While multiple sites of lysine methylation have been linked with gene activation, each modification is distributed to unique positions across the active gene. (PMID: 17030614, 1122639, 15756599, 3111294). N(6)-Methyllysine is a naturally occurring amino acid found in human biofluids. N-monomethyl-lysine is generated by metabolic transmethylation of endogenous lysine.

Isoputreanine

N-(3-Aminopropyl)-4-aminobutanoic acid

C7H16N2O2 (160.12117160000003)

Isoputreanine is urinary metabolite of spermidine, which is predominantly excreted as the monoacetyl conjugate of N-(3-aminopropyl)pyrrolidin-2-one, the acetylated γ-lactam form of isoputreanine. A human metabolite taken as a putative food compound of mammalian origin [HMDB]

N2-Methyl-L-lysine

(2S)-6-amino-2-(methylamino)hexanoic acid

C7H16N2O2 (160.12117160000003)

N2-Methyl-L-lysine, also known as N(a)-methyl-L-lysine, belongs to the class of organic compounds known as l-alpha-amino acids. Lysine methylation displays the highest degree of complexity among known covalent histone modifications, with each site of methylation regulating the association of different effector molecules. The versatility of lysine methylation marks is perhaps best exemplified by modifications implicated in transcriptional regulation as well as being required for double-strand break repair in several organisms. Identification of the numerous biological functions encoded by histone lysine methylation is a major area of research interest. (PMID: 32119527)