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Identification
YMDB IDYMDB00028
NameN-Acetylornithine
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionN-Acetylornithine is an intermediate in the enzymatic biosynthesis of the amino acid L-arginine from L-glutamate.
Structure
Thumb
Synonyms
  • (2S)-2-acetamido-5-aminopentanoate
  • (2S)-2-acetamido-5-aminopentanoic acid
  • Acetyl-ornithine
  • AOR
  • delta-N-Acetylornithine
  • N(2)-acetyl-L-ornithine
  • N(delta)-Acetylornithine
  • N(delta)-Acetylornithine, (DL)-isomer
  • N2-Acetyl-L-ornithine
CAS number6205-08-9
WeightAverage: 174.1977
Monoisotopic: 174.100442324
InChI KeyJRLGPAXAGHMNOL-LURJTMIESA-N
InChIInChI=1S/C7H14N2O3/c1-5(10)9-6(7(11)12)3-2-4-8/h6H,2-4,8H2,1H3,(H,9,10)(H,11,12)/t6-/m0/s1
IUPAC Name(2S)-5-amino-2-acetamidopentanoic acid
Traditional IUPAC NameN(2)-acetyl-L-ornithine
Chemical FormulaC7H14N2O3
SMILES[H]OC(=O)[C@@]([H])(N([H])C(=O)C([H])([H])[H])C([H])([H])C([H])([H])C([H])([H])N([H])[H]
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
  • Fatty acid
  • Acetamide
  • Carboxamide group
  • Secondary carboxylic acid amide
  • Amino acid
  • Monocarboxylic acid or derivatives
  • Carboxylic acid
  • Organopnictogen compound
  • Organic oxygen compound
  • Organic nitrogen compound
  • Amine
  • Primary amine
  • Organooxygen compound
  • Organonitrogen compound
  • Primary aliphatic amine
  • Hydrocarbon derivative
  • Carbonyl group
  • Organic oxide
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting pointNot Available
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogP-0.896PhysProp
Predicted Properties
PropertyValueSource
Water Solubility37.8 g/LALOGPS
logP-2.7ALOGPS
logP-3.6ChemAxon
logS-0.66ALOGPS
pKa (Strongest Acidic)3.82ChemAxon
pKa (Strongest Basic)9.9ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area92.42 ŲChemAxon
Rotatable Bond Count5ChemAxon
Refractivity42.65 m³·mol⁻¹ChemAxon
Polarizability17.94 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • mitochondrion
Organoleptic PropertiesNot Available
SMPDB PathwaysNot Available
KEGG Pathways
Arginine and proline metabolismec00330 Map00330
SMPDB ReactionsNot Available
KEGG Reactions
2-Acetamido-5-oxopentanoic acid + L-Glutamic acidOxoglutaric acid + N-Acetylornithine
L-Glutamic acid + N-AcetylornithineN-acetyl-L-glutamic acid + Ornithine
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Liu, Y., Van Heeswijck, R., Hoj, P., Hoogenraad, N. (1995). "Purification and characterization of ornithine acetyltransferase from Saccharomyces cerevisiae." Eur J Biochem 228:291-296.7705341
  • Crabeel, M., Abadjieva, A., Hilven, P., Desimpelaere, J., Soetens, O. (1997). "Characterization of the Saccharomyces cerevisiae ARG7 gene encoding ornithine acetyltransferase, an enzyme also endowed with acetylglutamate synthase activity." Eur J Biochem 250:232-241.9428669
Synthesis Reference:Not Available
External Links:
ResourceLink
CHEBI ID16543
HMDB IDHMDB03357
Pubchem Compound ID439232
Kegg IDC00437
ChemSpider ID388369
FOODB IDFDB031020
Wikipedia IDNot Available
BioCyc IDN-ALPHA-ACETYLORNITHINE

Enzymes

General function:
Involved in transaminase activity
Specific function:
N(2)-acetyl-L-ornithine + 2-oxoglutarate = N- acetyl-L-glutamate 5-semialdehyde + L-glutamate
Gene Name:
ARG8
Uniprot ID:
P18544
Molecular weight:
46681.10156
Reactions
N(2)-acetyl-L-ornithine + 2-oxoglutarate → N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
General function:
Involved in glutamate N-acetyltransferase activity
Specific function:
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis:the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate
Gene Name:
ARG7
Uniprot ID:
Q04728
Molecular weight:
47848.30078
Reactions
N(2)-acetyl-L-ornithine + L-glutamate → L-ornithine + N-acetyl-L-glutamate.
Acetyl-CoA + L-glutamate → CoA + N-acetyl-L-glutamate.