MiMeDB: Showing metabocard for N-Acetyl-L-alanine (MMDBc0000541)

Record Information

Version

1.0

Status

Detected and Quantified

Creation Date

2020-12-10 18:40:07 UTC

Update Date

2024-10-09 22:11:40 UTC

Metabolite ID

MMDBc0000541

Metabolite Identification

Common Name

N-Acetyl-L-alanine

Description

N-Acetyl-L-alanine or N-Acetylalanine, 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-Acetyl-L-alanine can also be classified as an alpha amino acid or a derivatized alpha amino acid. Technically, N-alpha-Acetyl-L-alanine is a biologically available N-terminal capped form of the proteinogenic alpha amino acid L-alanine. 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-Acetyl-L-alanine is a product of the enzyme known as ribosomal alanine N-acetyltransferase (EC 2.3.1.128) which catalyzes the transfer of the acetyl group of acetyl CoA to proteins bearing an N-terminal alanine. N-acetylated amino acids, such as N-acetylalanine can be released by an N-acylpeptide hydrolase from peptides generated by proteolytic degradation (PMID: 16465618 ). Excessive amounts N-acetyl amino acids can be detected in the urine with individuals with aminoacylase I deficiency, a genetic disorder (PMID: 16465618 ). These include N-acetylalanine (as well as N-acetylserine, N-acetylglutamine, N-acetylglutamate, N-acetylglycine, N-acetylmethionine and smaller amounts of N-acetylthreonine, N-acetylleucine, N-acetylvaline and N-acetylisoleucine. 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-acetylalanine, are classified as uremic toxins (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-Acetyl-L-alanine has been identified in the human placenta (PMID: 32033212 ).

Structure

MOL SDF PDB SMILES InChI

Synonyms

Value	Source
(S)-2-(Acetylamino)propanoic acid	ChEBI
2-Acetamidopropionic acid	ChEBI
Ac-ala-OH	ChEBI
Acetylalanine	ChEBI
L-N-Acetylalanine	ChEBI
N-Acetyl-L-alpha-alanine	ChEBI
N-Acetyl-S-alanine	ChEBI
N-Acetylalanine	ChEBI
(S)-2-(Acetylamino)propanoate	Generator
2-Acetamidopropionate	Generator
N-Acetyl-L-a-alanine	Generator
N-Acetyl-L-α-alanine	Generator
(S)-(-)-N-Acetylalanine	HMDB
(S)-N-Acetylalanine	HMDB
Acetyl-L-alanine	HMDB
N-Acetyl-(S)-alanine	HMDB

Molecular Formula

C₅H₉NO₃

Average Mass

131.1299

Monoisotopic Mass

131.058243159

IUPAC Name

Not Available

Traditional Name

Not Available

CAS Registry Number

Not Available

SMILES

Not Available

InChI Identifier

InChI=1S/C5H9NO3/c1-3(5(8)9)6-4(2)7/h3H,1-2H3,(H,6,7)(H,8,9)/t3-/m0/s1

InChI Key

KTHDTJVBEPMMGL-VKHMYHEASA-N

Chemical Taxonomy

Description

Belongs to the class of organic compounds known as n-acyl-l-alpha-amino acids. These are n-acylated alpha amino acids which have the L-configuration of the alpha-carbon atom.

Kingdom

Organic compounds

Super Class

Organic acids and derivatives

Class

Carboxylic acids and derivatives

Sub Class

Amino acids, peptides, and analogues

Direct Parent

N-acyl-L-alpha-amino acids

Alternative Parents

Substituents

N-acyl-l-alpha-amino acid
Alanine or derivatives
Acetamide
Carboxamide group
Secondary carboxylic acid amide
Carboxylic acid
Monocarboxylic acid or derivatives
Organopnictogen compound
Organic oxygen compound
Organooxygen compound
Organonitrogen compound
Carbonyl group
Organic nitrogen compound
Organic oxide
Hydrocarbon derivative
Aliphatic acyclic compound

Molecular Framework

Aliphatic acyclic compounds

External Descriptors

L-alanine derivative (CHEBI:40992 )
N-acetyl-L-amino acid (CHEBI:40992 )

Functional Ontology

Not Available

Physical Properties

State

Expected Solid

Predicted Properties

Not Available

Spectra

Not Available

Biological Properties

Cellular Locations

Cytoplasm

Biospecimen Locations

Blood
Feces
Placenta
Urine

Tissue Locations

Placenta

Associated OMIM IDs

114500 (Colorectal cancer)
610247 (Eosinophilic esophagitis)

Human Proteins and Enzymes

Protein ID	Protein Name	Protein Type	Uniprot ID	Species
MMDBp0192027	Carbamoyl-phosphate synthase [ammonia], mitochondrial	Enzyme	P31327	Homo sapiens
MMDBp0192168	N-acetylglutamate synthase, mitochondrial	Enzyme	Q8N159	Homo sapiens

Human Pathways

Pathways

Name	SMPDB/PathBank

Metabolic Reactions

Reactions

Reaction ID	Precursor	Product	Enzyme	Reaction Type	Data Source	Reference
MMDBr0004150	L-Alanine	N-Acetyl-L-alanine	N-acetylglutamate synthase		VMH	12459178 12594532
MMDBr0004330	N-Acetyl-L-alanine	Acetic acid	Not Available		VMH	9518469

Health Effects and Bioactivity

Health Outcome/Bioactivity	Metabolite Response/Effect	Evidence Type	Host and Biospecimen	Data Source	Reference
Prostate cancer		Association	Human Urine	HMDB	19212411

Microbial Sources

Superkingdom/Kingdom	Phylum	Total species	Hosts and Body Sites	Microbial Links
Bacteria	Proteobacteria	1	Human feces; Human urine	Indirect association between microbiota composition and metabolites measured in host biospecimen
Bacteria	Firmicutes	8	Human feces; Human stool; Human ; Human urine; Human sputum	Indirect association between microbiota composition and metabolites measured in host biospecimen
Eukaryota/Fungi	Ascomycota	1	Human feces; Human saliva	Unknown

Exposure Sources

Source Type	Activity	Data Source	Reference
Drugs	Antimicrobial	U.S. Environmental Protection Agency	CompTox
Cosmetics	Not Available	U.S. Environmental Protection Agency	CompTox
Domestics	Not Available	U.S. Environmental Protection Agency	CompTox

Host Biospecimen and Location

Host and Biospecimen	Status	Mean	Min	Max	Units	Age	Sex	Health Condition	Data Source	Reference
Human Feces	Detected but not Quantified								HMDB
Human Urine	Detected and Quantified	0.5	0.0	1.0	umol/mmol creatinine	Adult (>18 years old)	Both	Prostate Cancer	HMDB	19212411
Human Placenta	Detected but not Quantified					Not Specified	Not Specified	Normal	HMDB	34986597
Human Feces	Detected but not Quantified					Adult (>18 years old)	Both	Normal	HMDB	27543620
Human Feces	Detected but not Quantified					Adult (>18 years old)	Both	Normal	HMDB	25037050
Human Feces	Detected but not Quantified					Adult (>18 years old)	Both	Normal	HMDB	29808030
Human Blood	Detected but not Quantified								HMDB

External Links

HMDB ID

HMDB0000766

DrugBank ID

DB02518

Phenol Explorer Compound ID

Not Available

FooDB ID

FDB022231

KNApSAcK ID

Not Available

Chemspider ID

79449

KEGG Compound ID

Not Available

BioCyc ID

Not Available

BiGG ID

Not Available

Wikipedia Link

Not Available

METLIN ID

5733

PubChem Compound

88064

PDB ID

Not Available

ChEBI ID

40992

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 ]
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-alanine (MMDBc0000541)

MOL for #<Metabolite:0x00007fdb58772d48>

3D MOL for #<Metabolite:0x00007fdb58772d48>

3D SDF for #<Metabolite:0x00007fdb58772d48>

3D-SDF for #<Metabolite:0x00007fdb58772d48>

PDB for #<Metabolite:0x00007fdb58772d48>

3D PDB for #<Metabolite:0x00007fdb58772d48>

SMILES for #<Metabolite:0x00007fdb58772d48>

INCHI for #<Metabolite:0x00007fdb58772d48>

Structure for #<Metabolite:0x00007fdb58772d48>

3D Structure for #<Metabolite:0x00007fdb58772d48>