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Fumaric acid (YMDB00101)

Identification
YMDB IDYMDB00101
NameFumaric acid
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionFumaric acid, also known as fumarate or E297, belongs to the class of organic compounds known as dicarboxylic acids and derivatives. These are organic compounds containing exactly two carboxylic acid groups. Fumaric acid is a weakly acidic compound (based on its pKa). Fumaric acid exists in all living species, ranging from bacteria to humans. Within yeast, fumaric acid participates in a number of enzymatic reactions. In particular, ubiquinol-1 and fumaric acid can be biosynthesized from succinic acid and ubiquinone-1 through its interaction with the enzyme succinate:quinone oxidoreductase. In addition, ubiquinol-1 and fumaric acid can be biosynthesized from succinic acid and ubiquinone-1; which is catalyzed by the enzyme succinate:quinone oxidoreductase. In yeast, fumaric acid is involved in the metabolic pathway called the oxidative phosphorylation pathway. Fumaric acid is a potentially toxic compound.
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
  • (2E)-2-Butenedioic acid
  • (2E)-But-2-enedioate
  • (2E)-But-2-enedioic acid
  • (E)-2-Butenedioate
  • (E)-2-Butenedioic acid
  • (E)-2-butenedioic acid, ion(2-)
  • (E)-HO2CCH=CHCO2H
  • 1, 2-Ethenedicarboxylic acid, trans-
  • 1,2-Ethenedicarboxylic acid, trans-
  • 1,2-Ethylenedicarboxylic acid, (E)
  • 2-(E)-Butenedioate
  • 2-(E)-Butenedioic acid
  • 2-butenedioic acid
  • 2-Butenedioic acid (E)-
  • 2-Butenedioic acid, (E)-
  • Allomaleate
  • Allomaleic acid
  • Boletate
  • Boletic acid
  • Butenedioic acid, (E)-
  • Fumarate
  • Fumaric acid
  • Kyselina fumarova
  • Lichenate
  • Lichenic acid
  • sodium fumarate
  • trans-1,2-Ethylenedicarboxylate
  • trans-1,2-Ethylenedicarboxylic acid
  • trans-2-Butenedioate
  • trans-2-Butenedioic acid
  • trans-Butenedioate
  • trans-Butenedioic acid
  • Tumaric acid
  • e297
  • Fumarsaeure
  • trans-But-2-enedioic acid
  • (2E)-2-Butenedioate
  • trans-But-2-enedioate
  • FC 33
  • Furamag
  • Ammonium fumarate
  • Magnesium fumarate
  • Mafusol
CAS number110-17-8
WeightAverage: 116.0722
Monoisotopic: 116.010958616
InChI KeyVZCYOOQTPOCHFL-OWOJBTEDSA-N
InChIInChI=1S/C4H4O4/c5-3(6)1-2-4(7)8/h1-2H,(H,5,6)(H,7,8)/b2-1+
IUPAC Name(2E)-but-2-enedioic acid
Traditional IUPAC Namefumaric acid
Chemical FormulaC4H4O4
SMILESOC(=O)\C=C\C(O)=O
Chemical Taxonomy
Description belongs to the class of organic compounds known as dicarboxylic acids and derivatives. These are organic compounds containing exactly two carboxylic acid groups.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassDicarboxylic acids and derivatives
Direct ParentDicarboxylic acids and derivatives
Alternative Parents
Substituents
  • Fatty acyl
  • Fatty acid
  • Unsaturated fatty acid
  • Dicarboxylic acid or derivatives
  • Carboxylic acid
  • Organic oxygen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Organooxygen compound
  • Carbonyl group
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
StateSolid
Charge0
Melting point549 °C
Experimental Properties
PropertyValueReference
Water Solubility7 mg/mL at 25 oC [US EPA (1981)]PhysProp
LogP0.46 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
logP-0.041ChemAxon
pKa (Strongest Acidic)3.55ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area74.6 ŲChemAxon
Rotatable Bond Count2ChemAxon
Refractivity24.61 m³·mol⁻¹ChemAxon
Polarizability9.35 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Mitochondrion
Organoleptic Properties
Flavour/OdourSource
OdorlessFDB008113
SourFDB008113
SMPDB Pathways
Citric Acid CyclePW000952 ThumbThumb?image type=greyscaleThumb?image type=simple
Citric Acid Cycle 1434561204PW000970 ThumbThumb?image type=greyscaleThumb?image type=simple
Oxidative phosphorylationPW002461 ThumbThumb?image type=greyscaleThumb?image type=simple
Phenylalanine metabolismPW002437 ThumbThumb?image type=greyscaleThumb?image type=simple
TCA CyclePW002377 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Alanine, aspartate and glutamate metabolismec00250 Map00250
Arginine and proline metabolismec00330 Map00330
Butanoate metabolismec00650 Map00650
Citrate cycle (TCA cycle)ec00020 Map00020
Nicotinate and nicotinamide metabolismec00760 Map00760
SMPDB Reactions
(S)-Malic acid ↔ Fumaric acid + water
Succinic acid + Coenzyme Q10 + FAD ↔ Fumaric acid + QH2 + FADH2
L-Aspartic acid → Fumaric acid + Ammonia
Adenylsuccinic acid → Fumaric acid + Adenosine monophosphate
Argininosuccinic acid → Fumaric acid + L-Arginine
KEGG Reactions
SAICAR ↔ 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide + Fumaric acid
Adenylsuccinic acid ↔ Adenosine monophosphate + Fumaric acid
Argininosuccinic acid ↔ L-Arginine + Fumaric acid
Fumaric acid + water ↔ (S)-malate(2-)
Fumaric acid + L-Dihydroorotic acid → Orotic acid + Succinic acid
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
  • Peleg, Y., Rokem, J. S., Goldberg, I., Pines, O. (1990). "Inducible overexpression of the FUM1 gene in Saccharomyces cerevisiae: localization of fumarase and efficient fumaric acid bioconversion to L-malic acid." Appl Environ Microbiol 56:2777-2783.2275532
  • Palmieri, L., Lasorsa, F. M., De Palma, A., Palmieri, F., Runswick, M. J., Walker, J. E. (1997). "Identification of the yeast ACR1 gene product as a succinate-fumarate transporter essential for growth on ethanol or acetate." FEBS Lett 417:114-118.9395087
  • Przybyla-Zawislak, B., Gadde, D. M., Ducharme, K., McCammon, M. T. (1999). "Genetic and biochemical interactions involving tricarboxylic acid cycle (TCA) function using a collection of mutants defective in all TCA cycle genes." Genetics 152:153-166.10224250
  • Nagy, M., Lacroute, F., Thomas, D. (1992). "Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts." Proc Natl Acad Sci U S A 89:8966-8970.1409592
  • Muratsubaki, H., Enomoto, K. (1998). "One of the fumarate reductase isoenzymes from Saccharomyces cerevisiae is encoded by the OSM1 gene." Arch Biochem Biophys 352:175-181.9587404
  • Castrillo, J. I., Zeef, L. A., Hoyle, D. C., Zhang, N., Hayes, A., Gardner, D. C., Cornell, M. J., Petty, J., Hakes, L., Wardleworth, L., Rash, B., Brown, M., Dunn, W. B., Broadhurst, D., O'Donoghue, K., Hester, S. S., Dunkley, T. P., Hart, S. R., Swainston, N., Li, P., Gaskell, S. J., Paton, N. W., Lilley, K. S., Kell, D. B., Oliver, S. G. (2007). "Growth control of the eukaryote cell: a systems biology study in yeast." J Biol 6:4.17439666
Synthesis Reference:Dong, Changsheng; Ma, Xinming. Method for preparation of fumaric acid from the tail gas acid spray solution from oxidation of phthalic anhydride. Faming Zhuanli Shenqing Gongkai Shuomingshu (2007), 5pp.
External Links:
ResourceLink
CHEBI ID18012
HMDB IDHMDB00134
Pubchem Compound ID723
Kegg IDC00122
ChemSpider ID24532688
FOODB IDFDB008113
WikipediaFumaric_acid
BioCyc IDFUM

Enzymes

Protein Details
1. Adenylosuccinate lyase
General function:
Involved in catalytic activity
Specific function:
N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP
Gene Name:
ADE13
Uniprot ID:
Q05911
Molecular weight:
54509.89844
Reactions
N(6)-(1,2-dicarboxyethyl)AMP → fumarate + AMP.
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate → fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Protein Details
2. Argininosuccinate lyase
General function:
Involved in argininosuccinate lyase activity
Specific function:
2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
Gene Name:
ARG4
Uniprot ID:
P04076
Molecular weight:
51988.69922
Reactions
2-(N(omega)-L-arginino)succinate → fumarate + L-arginine.
Protein Details
3. Fumarate reductase
General function:
Involved in electron carrier activity
Specific function:
Could be a fumarate reductase
Gene Name:
Not Available
Uniprot ID:
P32614
Molecular weight:
50843.69922
Reactions
Succinate + NAD(+) → fumarate + NADH.
Protein Details
4. Osmotic growth protein 1
General function:
Involved in electron carrier activity
Specific function:
Could be a fumarate reductase
Gene Name:
OSM1
Uniprot ID:
P21375
Molecular weight:
55064.80078
Reactions
Protein Details
5. Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
General function:
Involved in electron carrier activity
Specific function:
Catalytic subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic dimer. Electrons flow from succinate to the FAD bound to SDH1, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4
Gene Name:
SDH1
Uniprot ID:
Q00711
Molecular weight:
70228.79688
Reactions
Succinate + ubiquinone → fumarate + ubiquinol.
Protein Details
6. Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial
General function:
Involved in electron carrier activity
Specific function:
Probable minor catalytic subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Probably forms a catalytic dimer with SDH2. Electrons flow from succinate to the FAD bound to the catalytic subunit, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4
Gene Name:
Not Available
Uniprot ID:
P47052
Molecular weight:
69382.0
Reactions
Succinate + ubiquinone → fumarate + ubiquinol.
Protein Details
7. Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
General function:
Involved in 2 iron, 2 sulfur cluster binding
Specific function:
Subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic dimer. Electrons flow from succinate to the FAD bound to SDH1, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4
Gene Name:
SDH2
Uniprot ID:
P21801
Molecular weight:
30230.90039
Reactions
Succinate + ubiquinone → fumarate + ubiquinol.
Protein Details
8. Fumarate hydratase, mitochondrial
General function:
Involved in fumarate hydratase activity
Specific function:
(S)-malate = fumarate + H(2)O
Gene Name:
FUM1
Uniprot ID:
P08417
Molecular weight:
53151.5
Reactions
(S)-malate → fumarate + H(2)O.
Protein Details
9. Dihydroorotate dehydrogenase
General function:
Involved in catalytic activity
Specific function:
In the de novo pyrimidine biosynthesic pathway, catalyzes the stereospecific oxidation of (S)-dihydroorotate to orotate and the reduction of fumarate to succinate. Does not use oxaloacetate and NAD or NADP as electron acceptors
Gene Name:
URA1
Uniprot ID:
P28272
Molecular weight:
34800.60156
Reactions
(S)-dihydroorotate + O(2) → orotate + H(2)O(2).
(S)-dihydroorotate + a quinone → orotate + a quinol

Transporters

Protein Details
1. Succinate/fumarate mitochondrial transporter
General function:
Involved in binding
Specific function:
Transports cytoplasmic succinate, derived from isocitrate by the action of isocitrate lyase in the cytosol, into the mitochondrial matrix in exchange for fumarate
Gene Name:
SFC1
Uniprot ID:
P33303
Molecular weight:
35340.10156