MiMeDB: Showing metabocard for N-Acetyl-L-methionine (MMDBc0000457)

Record Information

Version

1.0

Status

Detected and Quantified

Creation Date

2020-12-10 18:38:12 UTC

Update Date

2022-08-31 06:06:58 UTC

MiMeDB ID

MMDBc0000457

Metabolite Identification

Common Name

N-Acetyl-L-methionine

Description

N-Acetyl-L-methionine or N-Acetylmethionine, 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-Acetylmethionine can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-Acetylmethionine is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-methionine. 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-acetylmethionine 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 methionine can also occur. In particular, N-Acetylmethionine can be biosynthesized from L-methionine and acetyl-CoA by the enzyme methionine N-acetyltransferase (EC 2.3.1.66). Excessive amounts N-acetyl amino acids including N-acetylmethionine (as well as N-acetylglycine, N-acetylserine, N-acetylglutamine, 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-acetylmethionine 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 ).

Structure

MOL SDF PDB SMILES InChI

Synonyms

Not Available

Chemical Formula

C₇H₁₃NO₃S

Average Molecular Weight

191.248

Monoisotopic Molecular Weight

191.061613977

IUPAC Name

Not Available

Traditional Name

Not Available

CAS Registry Number

Not Available

SMILES

Not Available

InChI Identifier

InChI=1S/C7H13NO3S/c1-5(9)8-6(7(10)11)3-4-12-2/h6H,3-4H2,1-2H3,(H,8,9)(H,10,11)/t6-/m0/s1

InChI Key

XUYPXLNMDZIRQH-LURJTMIESA-N

Chemical Taxonomy

Functional Ontology

Not Available

Physical Properties

State

Expected Solid

Predicted Properties

Not Available

Spectra

Not Available

Biological Properties

Cellular Locations

Not Available

Biospecimen Locations

Feces
Placenta
Saliva

Tissue Locations

Placenta

Associated OMIM IDs

114500 (Colorectal cancer)
610247 (Eosinophilic esophagitis)

Human Proteins and Enzymes

Proteins

#<MetaboliteProteinLink:0x000055b76e09bd90>

Human Pathways

Pathways

Name	SMPDB/PathBank

Metabolic Reactions

Reaction ID	Precursor	Product	Enzyme	Reaction Type	Data Source	Reference

Health Effects and Bioactivity

Health Outcome/Bioactivity	Metabolite Response/Effect	Related Health Condition	Evidence Type	Measured in Matrix	Data Source	Reference

Microbial Sources

Phylum	Total species	Hosts and Body Sites	Microbial Links
Verrucomicrobia	1	Human Feces	Indirect association between microbiota composition and metabolites measured in host biospecimen
Bacteroidetes	1	Human Appendix biopsy	Indirect association between microbiota composition and metabolites measured in host biospecimen
Firmicutes	9	Human	Indirect association between microbiota composition and metabolites measured in host biospecimen

Exposure Sources

Source Type	Source Sub-type	Species	Data Source	Reference	Details

Host Biospecimen and Location

Host and Biospecimen	Status	Age	Sex	Health Condition	Data Source	Reference
Human Feces	Detected but not Quantified				HMDB		details
Human Placenta	Detected but not Quantified	Not Specified	Not Specified	Normal	HMDB	34986597	details
Human Saliva	Detected but not Quantified	Adult (>18 years old)	Male	Normal	HMDB	22308371	details
Human Saliva	Detected but not Quantified	Adult (>18 years old)	Male	Normal	HMDB	22308371	details
Human Saliva	Detected but not Quantified	Adult (>18 years old)	Male	Normal	HMDB	22308371	details
Human Saliva	Detected but not Quantified	Adult (>18 years old)	Male	Normal	HMDB	22308371	details
Human Saliva	Detected but not Quantified	Adult (>18 years old)	Male	Normal	HMDB	22308371	details
Human Saliva	Detected but not Quantified	Adult (>18 years old)	Male	Normal	HMDB	22308371	details
Human Saliva	Detected but not Quantified	Adult (>18 years old)	Male	Normal	HMDB	22308371	details
Human Saliva	Detected but not Quantified	Adult (>18 years old)	Male	Normal	HMDB	22308371	details
Human Saliva	Detected but not Quantified	Adult (>18 years old)	Male	Normal	HMDB	22308371	details
Human Saliva	Detected but not Quantified	Adult (>18 years old)	Male	Normal	HMDB	22308371	details
Human Feces	Detected but not Quantified	Adult (>18 years old)	Both	Normal	HMDB	27543620	details
Human Feces	Detected but not Quantified	Adult (>18 years old)	Both	Normal	HMDB	25037050	details
Human Feces	Detected but not Quantified	Adult (>18 years old)	Both	Normal	HMDB	29808030	details

External Links

HMDB ID

Not Available

DrugBank ID

Not Available

Phenol Explorer Compound ID

Not Available

FooDB ID

Not Available

KNApSAcK ID

Not Available

Chemspider ID

Not Available

KEGG Compound ID

Not Available

BioCyc ID

Not Available

BiGG ID

Not Available

Wikipedia Link

Not Available

METLIN ID

Not Available

PubChem Compound

Not Available

PDB ID

Not Available

ChEBI ID

Not Available

Food Biomarker Ontology

Not Available

References

Synthesis Reference

Not Available

General References

Sass JO, Mohr V, Olbrich H, Engelke U, Horvath J, Fliegauf M, Loges NT, Schweitzer-Krantz S, Moebus R, Weiler P, Kispert A, Superti-Furga A, Wevers RA, Omran H: Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism. Am J Hum Genet. 2006 Mar;78(3):401-9. doi: 10.1086/500563. Epub 2006 Jan 18. [PubMed:16465618 ]
Ball RO, Courtney-Martin G, Pencharz PB: The in vivo sparing of methionine by cysteine in sulfur amino acid requirements in animal models and adult humans. J Nutr. 2006 Jun;136(6 Suppl):1682S-1693S. doi: 10.1093/jn/136.6.1682S. [PubMed:16702340 ]
van de Poll MC, Dejong CH, Soeters PB: Adequate range for sulfur-containing amino acids and biomarkers for their excess: lessons from enteral and parenteral nutrition. J Nutr. 2006 Jun;136(6 Suppl):1694S-1700S. doi: 10.1093/jn/136.6.1694S. [PubMed:16702341 ]
Garlick PJ: Toxicity of methionine in humans. J Nutr. 2006 Jun;136(6 Suppl):1722S-1725S. doi: 10.1093/jn/136.6.1722S. [PubMed:16702346 ]
Vanholder R, Baurmeister U, Brunet P, Cohen G, Glorieux G, Jankowski J: A bench to bedside view of uremic toxins. J Am Soc Nephrol. 2008 May;19(5):863-70. doi: 10.1681/ASN.2007121377. Epub 2008 Feb 20. [PubMed:18287557 ]
Toyohara T, Akiyama Y, Suzuki T, Takeuchi Y, Mishima E, Tanemoto M, Momose A, Toki N, Sato H, Nakayama M, Hozawa A, Tsuji I, Ito S, Soga T, Abe T: Metabolomic profiling of uremic solutes in CKD patients. Hypertens Res. 2010 Sep;33(9):944-52. doi: 10.1038/hr.2010.113. Epub 2010 Jul 8. [PubMed:20613759 ]
Van Damme P, Hole K, Pimenta-Marques A, Helsens K, Vandekerckhove J, Martinho RG, Gevaert K, Arnesen T: NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet. 2011 Jul;7(7):e1002169. doi: 10.1371/journal.pgen.1002169. Epub 2011 Jul 7. [PubMed:21750686 ]
Tanaka H, Sirich TL, Plummer NS, Weaver DS, Meyer TW: An Enlarged Profile of Uremic Solutes. PLoS One. 2015 Aug 28;10(8):e0135657. doi: 10.1371/journal.pone.0135657. eCollection 2015. [PubMed:26317986 ]
Ree R, Varland S, Arnesen T: Spotlight on protein N-terminal acetylation. Exp Mol Med. 2018 Jul 27;50(7):1-13. doi: 10.1038/s12276-018-0116-z. [PubMed:30054468 ]
Elshenawy S, Pinney SE, Stuart T, Doulias PT, Zura G, Parry S, Elovitz MA, Bennett MJ, Bansal A, Strauss JF 3rd, Ischiropoulos H, Simmons RA: The Metabolomic Signature of the Placenta in Spontaneous Preterm Birth. Int J Mol Sci. 2020 Feb 4;21(3). pii: ijms21031043. doi: 10.3390/ijms21031043. [PubMed:32033212 ]

Showing metabocard for N-Acetyl-L-methionine (MMDBc0000457)

MOL for #<Metabolite:0x000055b76e29c7c0>

3D MOL for #<Metabolite:0x000055b76e29c7c0>

3D SDF for #<Metabolite:0x000055b76e29c7c0>

3D-SDF for #<Metabolite:0x000055b76e29c7c0>

PDB for #<Metabolite:0x000055b76e29c7c0>

3D PDB for #<Metabolite:0x000055b76e29c7c0>

SMILES for #<Metabolite:0x000055b76e29c7c0>

INCHI for #<Metabolite:0x000055b76e29c7c0>

Structure for #<Metabolite:0x000055b76e29c7c0>

3D Structure for #<Metabolite:0x000055b76e29c7c0>