CHEBI:17981 - O-acetyl-L-serine

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ChEBI Name O-acetyl-L-serine ChEBI ID CHEBI:17981 ChEBI ASCII Name O-acetyl-L-serine Definition An acetyl-L-serine where the acetyl group is attached to the side-chain oxygen. It is an intermediate in the biosynthesis of the amino acid cysteine in bacteria. Stars This entity has been manually annotated by the ChEBI Team. Secondary ChEBI IDs CHEBI:12724, CHEBI:7668, CHEBI:44568, CHEBI:12710, CHEBI:12685, CHEBI:21938 Supplier Information We are unable to retrieve the vendor information for this entry at this time. Please try again later. Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Wikipedia License O-Acetylserine is an α-amino acid with the chemical formula HO2CCH(NH2)CH2OC(O)CH3. It is an intermediate in the biosynthesis of the common amino acid cysteine in bacteria and plants. O-Acetylserine is biosynthesized by acetylation of the serine by the enzyme serine transacetylase. The enzyme O-acetylserine (thiol)-lyase, using sulfide sources, converts this ester into cysteine, releasing acetate: HO2CCH(NH2)CH2OH → HO2CCH(NH2)CH2OC(O)CH3 HO2CCH(NH2)CH2OC(O)CH3 → HO2CCH(NH2)CH2SH Read full article at Wikipedia Formula C5H9NO4 Net Charge 0 Average Mass 147.12930 Monoisotopic Mass 147.05316 InChI InChI=1S/C5H9NO4/c1-3(7)10-2-4(6)5(8)9/h4H,2,6H2,1H3,(H,8,9)/t4-/m0/s1 InChIKey VZXPDPZARILFQX-BYPYZUCNSA-N SMILES CC(=O)OC[C@H](N)C(O)=O Metabolite of Species Details Saccharomyces cerevisiae (NCBI:txid4932) Source: yeast.sf.net See: PubMed Escherichia coli (NCBI:txid562) See: PubMed Homo sapiens (NCBI:txid9606) See: DOI Homo sapiens (NCBI:txid9606) See: MetaboLights Study Roles Classification Biological Role(s): Saccharomyces cerevisiae metabolite Any fungal metabolite produced during a metabolic reaction in Baker's yeast (Saccharomyces cerevisiae ). bacterial metabolite Any prokaryotic metabolite produced during a metabolic reaction in bacteria. View more via ChEBI Ontology ChEBI Ontology Outgoing O-acetyl-L-serine (CHEBI:17981) has role Saccharomyces cerevisiae metabolite (CHEBI:75772) O-acetyl-L-serine (CHEBI:17981) has role bacterial metabolite (CHEBI:76969) O-acetyl-L-serine (CHEBI:17981) is a acetate ester (CHEBI:47622) O-acetyl-L-serine (CHEBI:17981) is a acetyl-L-serine (CHEBI:22194) O-acetyl-L-serine (CHEBI:17981) is tautomer of O-acetyl-L-serine zwitterion (CHEBI:58340) Incoming O-acetyl-L-serine residue (CHEBI:141128) is substituent group from O-acetyl-L-serine (CHEBI:17981) O-acetyl-L-serine zwitterion (CHEBI:58340) is tautomer of O-acetyl-L-serine (CHEBI:17981) IUPAC Name O-acetyl-L-serine Synonyms Sources L-Serine, acetate (ester) ChemIDplus O-acetyl-L-serine ChEBI O-Acetyl-L-serine KEGG COMPOUND O3-acetyl-L-serine ChEBI O3-Acetyl-L-serine KEGG COMPOUND Manual Xrefs Databases ACETYLSERINE MetaCyc C00007459 KNApSAcK C00979 KEGG COMPOUND DB01837 DrugBank HMDB0003011 HMDB O-Acetylserine Wikipedia OAS PDBeChem View more database links Registry Numbers Types Sources 1723791 Reaxys Registry Number Reaxys 5147-00-2 CAS Registry Number KEGG COMPOUND 5147-00-2 CAS Registry Number ChemIDplus Citation Qiu J, Wang D, Ma Y, Jiang T, Xin Y (2013) Identification and characterization of serine acetyltransferase encoded by the Mycobacterium tuberculosis Rv2335 gene. International journal of molecular medicine 31, 1229-1233 [PubMed:23483228] [show Abstract] Serine acetyltransferase (CysE) is the first enzyme involved in the two-step enzymatic pathway of L-cysteine biosynthesis in bacteria and plants, but not in humans. CysE catalyzes the biosynthesis of O-acetyl-L-serine and CoA from L-serine (L-Ser) and acetyl-CoA (AcCoA). Mycobacterium tuberculosis (M. tuberculosis) Rv2335 was predicted as the cysE gene encoding serine acetyltransferase. In this study, the M. tuberculosis Rv2335 gene was cloned and the CysE protein was expressed in E. coli BL21 (DE3). The M. tuberculosis CysE protein was purified by Ni(2+) affinity chromatography and confirmed by SDS-PAGE, western blotting and mass spectrometry. The serine acetyltransferase activity of the M. tuberculosis CysE protein was detected using Ellman's reagent. M. tuberculosis CysE displayed optimal activity at pH 7.5 and 37˚C. The Michaelis constant for AcCoA and L-Ser was 0.0513±0.0050 and 0.0264±0.0006 mM, respectively. The maximum velocity (V(max)) for CysE was 0.0073±0.0005 mM/min. The CysE assay and the determination of the kinetic parameters of M. tuberculosis CysE may be helpful for screening its inhibitors in anti-tuberculosis drug discovery. Last Modified 12 February 2016