Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
twitter

Escherichia coli K-12 substr. MG1655 Compound: oxalate

Synonyms: oxalic acid, ethanedioic acid

Summary from MetaCyc:
Oxalate is the most oxidized two-carbon compound. It is made in high concentrations by some plants and fungi and can reach high micromolar concentrations in soil. Oxalate is toxic to mammals but is metabolized by many bacteria and plants by various pathways. In high concentrations, it causes death in humans and animals because of its corrosive effects, while smaller amounts can cause various pathological disorders, including hyperoxaluria, calcium oxalate stones, pyridoxine deficiency, and even renal failure.

Chemical Formula: C2O4

Molecular Weight: 88.02 Daltons

Monoisotopic Molecular Weight: 89.9953085526 Daltons

SMILES: C([O-])(C(=O)[O-])=O

InChI: InChI=1S/C2H2O4/c3-1(4)2(5)6/h(H,3,4)(H,5,6)/p-2

InChIKey: InChIKey=MUBZPKHOEPUJKR-UHFFFAOYSA-L

Unification Links: CAS:144-62-7 , ChEBI:30623 , ChemSpider:64235 , HMDB:HMDB02329 , KEGG:C00209 , MetaboLights:MTBLC30623 , PubChem:71081

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -161.1

In Reactions of unknown directionality:

Not in pathways:
acetyl-CoA + oxalate = oxalyl-CoA + acetate
formyl-CoA + oxalate = formate + oxalyl-CoA

Enzymes inhibited by oxalate, sorted by the type of inhibition, are:

Inhibitor (Competitive) of: glutamate decarboxylase B [Fonda72] , D-lactate dehydrogenase [Kaczorowski78] , isocitrate lyase [Comment 1] , cyanase [Anderson87, Comment 2] , malate synthase G [Falmagne65] , glutamate decarboxylase A [Fonda72]

Inhibitor (Mechanism unknown) of: 2-oxopent-4-enoate hydratase [Pollard98] , phosphoenolpyruvate synthetase [Narindrasorasak78] , formyl-CoA transferase [Toyota08] , pH 2.5 acid phosphatase [Dassa82, Comment 3]

In Growth Media: PMA carbon source test + oxalate


References

Anderson87: Anderson PM, Johnson WV, Endrizzi JA, Little RM, Korte JJ (1987). "Interaction of mono- and dianions with cyanase: evidence for apparent half-site binding." Biochemistry 26(13);3938-43. PMID: 3651424

Dassa82: Dassa E, Cahu M, Desjoyaux-Cherel B, Boquet PL (1982). "The acid phosphatase with optimum pH of 2.5 of Escherichia coli. Physiological and Biochemical study." J Biol Chem 1982;257(12);6669-76. PMID: 6282821

Falmagne65: Falmagne P, Vanderwinkel E, Wiame JM (1965). "Mise en evidence de deux malate synthases chez E. coli." BBActa 1965;99:246-258. PMID: 14336062

Fonda72: Fonda ML (1972). "Glutamate decarboxylase. Substrate specificity and inhibition by carboxylic acids." Biochemistry 1972;11(7);1304-9. PMID: 4552052

Hoyt88: Hoyt JC, Robertson EF, Berlyn KA, Reeves HC (1988). "Escherichia coli isocitrate lyase: properties and comparisons." Biochim Biophys Acta 1988;966(1);30-5. PMID: 3291954

Kaczorowski78: Kaczorowski G, Kohn LD, Kaback HR (1978). "Purification and properties of D-lactate dehydrogenase from Escherichia coli ML 308-225." Methods Enzymol 1978;53;519-27. PMID: 362128

Narindrasorasak78: Narindrasorasak S, Bridger WA (1978). "Probes of the structure of phosphoenolpyruvate synthetase: effects of a transition state analogue on enzyme conformation." Can J Biochem 56(8);816-9. PMID: 210911

Pollard98: Pollard JR, Bugg TD (1998). "Purification, characterisation and reaction mechanism of monofunctional 2-hydroxypentadienoic acid hydratase from Escherichia coli." Eur J Biochem 251(1-2);98-106. PMID: 9492273

Toyota08: Toyota CG, Berthold CL, Gruez A, Jonsson S, Lindqvist Y, Cambillau C, Richards NG (2008). "Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferase." J Bacteriol 190(7):2556-64. PMID: 18245280


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, BIOCYC14B.