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4-Phospho-L-aspartic acid (YMDB00113)

Identification
YMDB IDYMDB00113
Name4-Phospho-L-aspartic acid
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionL-Aspartyl-4-phosphate, also known as L-beta-aspartyl-p or phosphoaspartic acid, belongs to the class of organic compounds known as aspartic acid and derivatives. Aspartic acid and derivatives are compounds containing an aspartic acid or a derivative thereof resulting from reaction of aspartic acid at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom. In yeast, L-aspartyl-4-phosphate is involved in the metabolic pathway called the threonine metabolism pathway. Based on a literature review very few articles have been published on L-Aspartyl-4-phosphate.
Structure
Thumb
MOLSDF3D-SDFPDBSMILESInChI View 3D Structure
Synonyms
  • 4-phospho-L-aspartate
  • L-4-aspartyl phosphate
  • L-aspartyl-4-P
  • L-aspartyl-4-phosphate
  • L-aspartyl-b-phosphate
  • L-aspartyl-beta-phosphate
  • L-b-aspartyl-P
  • L-b-aspartyl-phosphate
  • L-beta-aspartyl-P
  • L-beta-aspartyl-phosphate
  • L-Aspart-4-yl phosphate
  • L-4-Aspartyl phosphoric acid
  • L-Aspart-4-yl phosphoric acid
  • L-Aspartyl-4-phosphoric acid
  • Phosphoaspartic acid
  • Aspartyl phosphate
  • beta-Aspartyl phosphate
  • 4-Phospho-L-aspartic acid
  • (2S)-2-Amino-4-oxo-4-(phosphonooxy)butanoic acid
  • 4-Phosphonato-L-aspartate
  • L-Aspartyl beta-phosphate
  • L-Aspartyl β-phosphate
  • L-Aspartyl-β-phosphate
  • L-Β-aspartyl-p
  • L-Β-aspartyl-phosphate
  • beta-L-Aspartyl phosphate
  • Β-aspartyl phosphate
  • Β-L-aspartyl phosphate
CAS number22138-53-0
WeightAverage: 213.0826
Monoisotopic: 213.003838127
InChI KeyIXZNKTPIYKDIGG-REOHCLBHSA-N
InChIInChI=1S/C4H8NO7P/c5-2(4(7)8)1-3(6)12-13(9,10)11/h2H,1,5H2,(H,7,8)(H2,9,10,11)/t2-/m0/s1
IUPAC Name(2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid
Traditional IUPAC Nameaspartyl phosphate
Chemical FormulaC4H8NO7P
SMILESN[C@@H](CC(=O)OP(O)(O)=O)C(O)=O
Chemical Taxonomy
Description belongs to the class of organic compounds known as aspartic acid and derivatives. Aspartic acid and derivatives are compounds containing an aspartic acid or a derivative thereof resulting from reaction of aspartic acid at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentAspartic acid and derivatives
Alternative Parents
Substituents
  • Aspartic acid or derivatives
  • Alpha-amino acid
  • L-alpha-amino acid
  • Acyl monophosphate
  • Acyl phosphate
  • Dicarboxylic acid or derivatives
  • Organic phosphoric acid derivative
  • Fatty acid
  • Carboxylic acid salt
  • Amino acid
  • Carboxylic acid
  • Primary amine
  • Organooxygen compound
  • Organonitrogen compound
  • Hydrocarbon derivative
  • Primary aliphatic amine
  • Organic oxide
  • Organic nitrogen compound
  • Organopnictogen compound
  • Carbonyl group
  • Amine
  • Organic oxygen compound
  • Organic salt
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting pointNot Available
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
Water Solubility13.2 g/LALOGPS
logP-1.9ALOGPS
logP-3.4ChemAxon
logS-1.2ALOGPS
pKa (Strongest Acidic)1.08ChemAxon
pKa (Strongest Basic)8.6ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count7ChemAxon
Hydrogen Donor Count4ChemAxon
Polar Surface Area147.15 ŲChemAxon
Rotatable Bond Count5ChemAxon
Refractivity37.69 m³·mol⁻¹ChemAxon
Polarizability16.08 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • Cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
Cysteine MetabolismPW002383 ThumbThumb?image type=greyscaleThumb?image type=simple
Methionine metabolism and salvagePW002384 ThumbThumb?image type=greyscaleThumb?image type=simple
threonine metabolismPW002401 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Cysteine and methionine metabolismec00270 Map00270
Glycine, serine and threonine metabolismec00260 Map00260
Lysine biosynthesisec00300 Map00300
SMPDB Reactions
4-Phospho-L-aspartic acid + hydron + NADPH → phosphate + NADP + L-aspartic 4-semialdehyde
Adenosine triphosphate + L-Aspartic acid → ADP + 4-Phospho-L-aspartic acid
L-Aspartic acid + Adenosine triphosphate → ADP + 4-Phospho-L-aspartic acid
4-Phospho-L-aspartic acid + NADPH + hydron → phosphate + NADP + L-aspartic 4-semialdehyde
KEGG Reactions
L-Aspartic acid + Adenosine triphosphate → 4-Phospho-L-aspartic acid + ADP
4-Phospho-L-aspartic acid + NADPH + hydron → NADP + phosphate + L-aspartic 4-semialdehyde
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0002-9100000000-a1228d9e19b509003dabJSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-00kb-5910000000-922e9c4170d8c8b3a82eJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-00xs-9400000000-136ddd947143dbaa3604JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0006-9000000000-f6bd39834e4c4068a518JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-004i-9120000000-3c9abfbc799f15bf7531JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-004i-9000000000-988aefb0bcb1d498234eJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-004i-9000000000-3845ebba5ef8ddf56b40JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0300-8950000000-318aca26c3ebeeab6749JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-00di-9100000000-b10f8d4da4a1d8226ec4JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-00dj-9000000000-b185b7cda6908131ad95JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-004i-9000000000-a5e502a2627af2048a1fJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-004i-9000000000-a5e502a2627af2048a1fJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-004i-9000000000-a5e502a2627af2048a1fJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
1D NMR13C NMR SpectrumNot AvailableJSpectraViewer
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
  • Thomas, D., Surdin-Kerjan, Y. (1989). "Structure of the HOM2 gene of Saccharomyces cerevisiae and regulation of its expression." Mol Gen Genet 217:149-154.2570346
Synthesis Reference:Not Available
External Links:
ResourceLink
CHEBI ID15836
HMDB IDHMDB12250
Pubchem Compound ID832
Kegg IDC03082
ChemSpider ID134354
FOODB IDFDB028892
Wikipedia IDNot Available
BioCyc IDL-BETA-ASPARTYL-P

Enzymes

Protein Details
1. Aspartate-semialdehyde dehydrogenase
General function:
Involved in aspartate-semialdehyde dehydrogenase activity
Specific function:
This enzyme catalyzes the second step in the common metabolic pathway to synthesize Thr and Met from Asp
Gene Name:
HOM2
Uniprot ID:
P13663
Molecular weight:
39543.30078
Reactions
L-aspartate 4-semialdehyde + phosphate + NADP(+) → L-4-aspartyl phosphate + NADPH.
Protein Details
2. Long-chain-fatty-acid--CoA ligase 4
General function:
Involved in catalytic activity
Specific function:
Esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Contributes, with FAA1, to the activation of imported myristate
Gene Name:
FAA4
Uniprot ID:
P47912
Molecular weight:
77266.5
Reactions
ATP + a long-chain carboxylic acid + CoA → AMP + diphosphate + an acyl-CoA.
Protein Details
3. Long-chain-fatty-acid--CoA ligase 1
General function:
Involved in catalytic activity
Specific function:
Esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. It may supplement intracellular myristoyl-CoA pools from exogenous myristate. Preferentially acts on C12:0-C16:0 fatty acids with myristic and pentadecanic acid (C15:0) having the highest activities
Gene Name:
FAA1
Uniprot ID:
P30624
Molecular weight:
77865.79688
Reactions
ATP + a long-chain carboxylic acid + CoA → AMP + diphosphate + an acyl-CoA.
Protein Details
4. Long-chain-fatty-acid--CoA ligase 3
General function:
Involved in catalytic activity
Specific function:
Esterification, concomitant with transport, of endogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. This enzyme acts preferentially on C16 and C18 fatty acids with a cis-double bond at C-9-C-10
Gene Name:
FAA3
Uniprot ID:
P39002
Molecular weight:
77946.0
Reactions
ATP + a long-chain carboxylic acid + CoA → AMP + diphosphate + an acyl-CoA.
Protein Details
5. Elongation of fatty acids protein 1
General function:
Involved in fatty acid elongase activity
Specific function:
May be a membrane bound enzyme involved in the highly specific elongation of saturated 14-carbon fatty acids (14:0) to 16-carbon species (16:0)
Gene Name:
ELO1
Uniprot ID:
P39540
Molecular weight:
36233.60156
Reactions
Acyl-CoA + malonyl-CoA → 3-oxoacyl-CoA + CoA + CO(2).
Protein Details
6. Fatty acid synthase subunit beta
General function:
Involved in transferase activity
Specific function:
Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for:[acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
Gene Name:
FAS1
Uniprot ID:
P07149
Molecular weight:
228689.0
Reactions
Acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH → long-chain-acyl-CoA + n CoA + n CO(2) + 2n NAD(+) + 2n NADP(+).
Acetyl-CoA + [acyl-carrier-protein] → CoA + acetyl-[acyl-carrier-protein].
Malonyl-CoA + [acyl-carrier-protein] → CoA + malonyl-[acyl-carrier-protein].
(3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] → hexadec-2-enoyl-[acyl-carrier-protein] + H(2)O.
Acyl-[acyl-carrier-protein] + NAD(+) → trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH.
Oleoyl-[acyl-carrier-protein] + H(2)O → [acyl-carrier-protein] + oleate.
Protein Details
7. Aspartokinase
General function:
Involved in amino acid binding
Specific function:
ATP + L-aspartate = ADP + 4-phospho-L- aspartate
Gene Name:
HOM3
Uniprot ID:
P10869
Molecular weight:
58109.19922
Reactions
ATP + L-aspartate → ADP + 4-phospho-L-aspartate.