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Record Information
Version4.0
StatusDetected and Quantified
Creation Date2006-05-22 15:12:20 UTC
Update Date2020-03-02 16:05:15 UTC
HMDB IDHMDB0002931
Secondary Accession Numbers
  • HMDB02931
Metabolite Identification
Common NameN-Acetylserine
DescriptionAcetylation of the N-terminal amino acid (-NH2 acetylation) is a common protein modification in eukaryotes but is rarely encountered in prokaryotes. In mammalians,80 to 90 percent of the cytosolic proteins are subjected to an irreversible, cotranslational amino acid acetylation at their N-terminus. Acetylation of the N-terminal amino acid (-NH2 acetylation) is a common protein modification in eukaryotes but is rarely encountered in prokaryotes. In mammalians, 80 to 90 percent of the cytosolic proteins are subjected to an irreversible, cotranslational amino acid acetylation at their N-terminus. N-acetylated proteins are catabolized in the cytosol by the ATP-ubiquitin-dependent proteasomal pathway. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase I (ACY1; EC 3.5.1.14), the most abundant type, is a soluble homodimeric zinc binding enzyme that catalyzes the formation of free aliphatic amino acids from N-acetylated precursors. It is encoded by the aminoacylase 1 gene (ACY1) on chromosome 3p21 that comprises 15 exons (OMIM 609924 ). Preferred substrates of ACY1 are aliphatic amino acids with a short-chain acyl moiety, especially N-acetyl-methionine. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. Functional aminoacylase I is crucial in the last step in this degradation as it catalyzes the hydrolysis of N-acetylated amino acids into acetate and the free amino acid. Although N-acetylation occurs in many metabolic pathways and N-acetylated metabolites are known to accumulate in several inborn errors, such as aminoacylase I deficiency. There are only a few reports on N-acetylated amino acids detected in urine. Identification of N-acetylated amino acids by routine GC-MS may be problematic for several reasons. The major problem is linked to the identification strategy itself. Identification of an unknown compound in mass spectrometry is usually based on comparison of its spectrum against a library of reference spectra (PMID: 16465618 , 16274666 , 17723438 ).
Structure
Data?1582752259
Synonyms
ValueSource
AcetylserineHMDB
N-Acetyl-L-serineHMDB
N-AcetylserineMeSH
(2S)-2-Acetamido-3-hydroxypropanoic acidHMDB
(2S)-2-Acetamido-3-hydroxypropionic acidHMDB
(S)-2-Acetamido-3-hydroxypropanoic acidHMDB
(S)-2-Acetamido-3-hydroxypropionic acidHMDB
Chemical FormulaC5H9NO4
Average Molecular Weight147.1293
Monoisotopic Molecular Weight147.053157781
IUPAC Name(2S)-2-acetamido-3-hydroxypropanoic acid
Traditional Nameacetylserine
CAS Registry Number16354-58-8
SMILES
CC(=O)N[C@@H](CO)C(O)=O
InChI Identifier
InChI=1S/C5H9NO4/c1-3(8)6-4(2-7)5(9)10/h4,7H,2H2,1H3,(H,6,8)(H,9,10)/t4-/m0/s1
InChI KeyJJIHLJJYMXLCOY-BYPYZUCNSA-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.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentN-acyl-L-alpha-amino acids
Alternative Parents
Substituents
  • N-acyl-l-alpha-amino acid
  • Serine or derivatives
  • Beta-hydroxy acid
  • Hydroxy acid
  • Acetamide
  • Carboxamide group
  • Secondary carboxylic acid amide
  • Carboxylic acid
  • Monocarboxylic acid or derivatives
  • Primary alcohol
  • Organooxygen compound
  • Organonitrogen compound
  • Organopnictogen compound
  • Alcohol
  • Organic oxygen compound
  • Carbonyl group
  • Organic nitrogen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Ontology
Physiological effect

Health effect:

Disposition

Route of exposure:

Source:

Biological location:

Role

Industrial application:

Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point207.6 °CNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility84.6 g/LALOGPS
logP-1.4ALOGPS
logP-1.8ChemAxon
logS-0.24ALOGPS
pKa (Strongest Acidic)3.61ChemAxon
pKa (Strongest Basic)-2ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area86.63 ŲChemAxon
Rotatable Bond Count3ChemAxon
Refractivity31.48 m³·mol⁻¹ChemAxon
Polarizability13.43 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Spectra
Spectrum TypeDescriptionSplash KeyView
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-0v4r-1910000000-55bfa57992b993e5736aSpectrum
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-0v4r-1910000000-55bfa57992b993e5736aSpectrum
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0006-9300000000-6b0aa9c8cd5d65af598eSpectrum
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (2 TMS) - 70eV, Positivesplash10-00dl-9640000000-e19818dfd1f671358afcSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-001j-2900000000-cbbd7e861694a1b35ef0Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0il9-9500000000-450a2fd0cc806534a001Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-001c-9000000000-92b250da801d4279b0ceSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0f6t-2900000000-4a518dea349294701f1dSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0ugs-9800000000-1fd980296f0d35c624aaSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0a4l-9100000000-b2ff3e9d761c45d69c15Spectrum
1D NMR1H NMR SpectrumNot AvailableSpectrum
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableSpectrum
Biological Properties
Cellular Locations
  • Cytoplasm (predicted from logP)
Biospecimen Locations
  • Feces
  • Saliva
  • Urine
Tissue Locations
  • Placenta
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
FecesDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Both
Normal
details
FecesDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Both
Normal
details
SalivaDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot QuantifiedAdult (>18 years old)Male
Normal
details
Abnormal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
UrineDetected and Quantified104 (99-111) umol/mmol creatinineAdult (>18 years old)Not SpecifiedAminoacylase I deficiency details
Associated Disorders and Diseases
Disease References
Aminoacylase I deficiency
  1. 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. Epub 2006 Jan 18. [PubMed:16465618 ]
Associated OMIM IDs
DrugBank IDDB02340
Phenol Explorer Compound IDNot Available
FooDB IDFDB000970
KNApSAcK IDNot Available
Chemspider ID58744
KEGG Compound IDNot Available
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkO-Acetylserine
METLIN ID308
PubChem Compound65249
PDB IDNot Available
ChEBI ID45441
Food Biomarker OntologyNot Available
VMH IDNot Available
References
Synthesis ReferenceTsurumi, Kohti; Yamada, Sakae. L-Serine from D-glucosamine. Tohoku Journal of Experimental Medicine (1955), 62 329-31.
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Boesgaard S, Aldershvile J, Poulsen HE, Christensen S, Dige-Petersen H, Giese J: N-acetylcysteine inhibits angiotensin converting enzyme in vivo. J Pharmacol Exp Ther. 1993 Jun;265(3):1239-44. [PubMed:8389858 ]
  2. Sugahara K, Zhang J, Kodama H: Liquid chromatographic-mass spectrometric analysis of N-acetylamino acids in human urine. J Chromatogr B Biomed Appl. 1994 Jul 1;657(1):15-21. [PubMed:7952062 ]
  3. Lynch AS, Tyrrell R, Smerdon SJ, Briggs GS, Wilkinson AJ: Characterization of the CysB protein of Klebsiella aerogenes: direct evidence that N-acetylserine rather than O-acetylserine serves as the inducer of the cysteine regulon. Biochem J. 1994 Apr 1;299 ( Pt 1):129-36. [PubMed:8166630 ]
  4. 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. Epub 2006 Jan 18. [PubMed:16465618 ]
  5. Van Coster RN, Gerlo EA, Giardina TG, Engelke UF, Smet JE, De Praeter CM, Meersschaut VA, De Meirleir LJ, Seneca SH, Devreese B, Leroy JG, Herga S, Perrier JP, Wevers RA, Lissens W: Aminoacylase I deficiency: a novel inborn error of metabolism. Biochem Biophys Res Commun. 2005 Dec 23;338(3):1322-6. Epub 2005 Nov 2. [PubMed:16274666 ]
  6. Gerlo E, Van Coster R, Lissens W, Winckelmans G, De Meirleir L, Wevers R: Gas chromatographic-mass spectrometric analysis of N-acetylated amino acids: the first case of aminoacylase I deficiency. Anal Chim Acta. 2006 Jul 7;571(2):191-9. Epub 2006 May 5. [PubMed:17723438 ]
  7. 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 ]

Enzymes

General function:
Involved in protein-glutamine gamma-glutamyltransferase activity
Specific function:
Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.
Gene Name:
F13A1
Uniprot ID:
P00488
Molecular weight:
83267.785
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284 ]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423 ]