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Record Information
Version3.6
Creation Date2006-05-22 15:12:20 UTC
Update Date2016-05-20 17:05:33 UTC
HMDB IDHMDB02931
Secondary Accession NumbersNone
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, 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
Thumb
Synonyms
ValueSource
AcetylserineHMDB
N-Acetyl-L-serineHMDB
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 KeyInChIKey=JJIHLJJYMXLCOY-BYPYZUCNSA-N
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as n-acyl-aliphatic-alpha amino acids. These are alpha amino acids carrying a N-acylated aliphatic chain.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentN-acyl-aliphatic-alpha amino acids
Alternative Parents
Substituents
  • N-acyl-aliphatic-alpha amino acid
  • N-acyl-l-alpha-amino acid
  • Beta-hydroxy acid
  • Hydroxy acid
  • Acetamide
  • Secondary carboxylic acid amide
  • Carboxamide group
  • Monocarboxylic acid or derivatives
  • Carboxylic acid
  • Carboxylic acid amide
  • Hydrocarbon derivative
  • Primary alcohol
  • Organooxygen compound
  • Organonitrogen compound
  • Carbonyl group
  • Alcohol
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External DescriptorsNot Available
Ontology
StatusDetected and Quantified
Origin
  • Endogenous
Biofunction
  • Protein synthesis, amino acid biosynthesis
ApplicationNot Available
Cellular locations
  • Cytoplasm (predicted from logP)
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 mg/mLALOGPS
logP-1.4ALOGPS
logP-1.8ChemAxon
logS-0.24ALOGPS
pKa (Strongest Acidic)3.61ChemAxon
pKa (Strongest Basic)-1.5ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area86.63 Å2ChemAxon
Rotatable Bond Count3ChemAxon
Refractivity31.48 m3·mol-1ChemAxon
Polarizability13.43 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-0v4r-1910000000-55bfa57992b993e5736aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-001j-2900000000-cbbd7e861694a1b35ef0View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0il9-9500000000-450a2fd0cc806534a001View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-001c-9000000000-92b250da801d4279b0ceView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0f6t-2900000000-4a518dea349294701f1dView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0ugs-9800000000-1fd980296f0d35c624aaView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0a4l-9100000000-b2ff3e9d761c45d69c15View in MoNA
1D NMR1H NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
Biological Properties
Cellular Locations
  • Cytoplasm (predicted from logP)
Biofluid Locations
  • Saliva
  • Urine
Tissue LocationNot Available
PathwaysNot Available
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
SalivaDetected but not QuantifiedNot ApplicableAdult (>18 years old)Male
Normal
details
Abnormal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
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. [16465618 ]
Associated OMIM IDs
DrugBank IDDB02340
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB000970
KNApSAcK IDNot Available
Chemspider ID58744
KEGG Compound IDNot Available
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkAcetylserine
NuGOwiki LinkHMDB02931
Metagene LinkHMDB02931
METLIN ID308
PubChem Compound65249
PDB IDSAC
ChEBI 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. 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. [16274666 ]
  2. 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. [16465618 ]
  3. 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. [7952062 ]
  4. 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. [8389858 ]
  5. 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. [8166630 ]
  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. [17723438 ]

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. [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. [17016423 ]
General function:
Involved in glycine N-acyltransferase activity
Specific function:
Mitochondrial acyltransferase which transfers an acyl group to the N-terminus of glycine and glutamine, although much less efficiently. Can conjugate numerous substrates to form a variety of N-acylglycines, with a preference for benzoyl-CoA over phenylacetyl-CoA as acyl donors. Thereby detoxify xenobiotics, such as benzoic acid or salicylic acid, and endogenous organic acids, such as isovaleric acid.
Gene Name:
GLYAT
Uniprot ID:
Q6IB77
Molecular weight:
18506.33
General function:
Involved in glycine N-acyltransferase activity
Specific function:
Acyltransferase which transfers an acyl group to the N-terminus of glutamine. Can use phenylacetyl-CoA as an acyl donor.
Gene Name:
GLYATL1
Uniprot ID:
Q969I3
Molecular weight:
35100.895
General function:
Involved in glycine N-acyltransferase activity
Specific function:
Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Conjugates numerous substrates, such as arachidonoyl-CoA and saturated medium and long-chain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA, to form a variety of N-acylglycines. Shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor. Does not exhibit any activity toward C22:6-CoA and chenodeoxycholoyl-CoA, nor toward serine or alanine.
Gene Name:
GLYATL2
Uniprot ID:
Q8WU03
Molecular weight:
34277.055