Escherichia coli K-12 substr. MG1655 Compound: hydroxypyruvate

Synonyms: β-hydroxypyruvate, OH-pyruvate, OH-pyr, 3-hydroxypyruvate

Chemical Formula: C3H3O4

Molecular Weight: 103.05 Daltons

Monoisotopic Molecular Weight: 104.0109586168 Daltons

hydroxypyruvate compound structure

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

InChI: InChI=1S/C3H4O4/c4-1-2(5)3(6)7/h4H,1H2,(H,6,7)/p-1


Unification Links: CAS:1113-60-6 , ChEBI:17180 , ChemSpider:3397158 , HMDB:HMDB01352 , IAF1260:34120 , KEGG:C00168 , MetaboLights:MTBLC17180 , PubChem:4186339

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -148.92

Reactions known to consume the compound:

Not in pathways:
D-glycerate + NADP+hydroxypyruvate + NADPH + H+

Reactions known to produce the compound:

Not in pathways:
3-phospho-hydroxypyruvate + H2O → hydroxypyruvate + phosphate

Reactions known to both consume and produce the compound:

Not in pathways:
hydroxypyruvate ↔ tartronate semialdehyde

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

Inhibitor (Competitive) of: pyruvate dehydrogenase [Bisswanger81] , 2-keto-4-hydroxyglutarate aldolase

Inhibitor (Irreversible) of: N-acetyl-β-neuraminate lyase [Lawrence97] , N-acetylneuraminate lyase [Lawrence97]

Inhibitor (Mechanism unknown) of: 4-hydroxy-tetrahydrodipicolinate synthase [Dobson08]

This compound has been characterized as an alternative substrate of the following enzymes: 3-phosphoserine aminotransferase , 4-hydroxy-tetrahydrodipicolinate synthase


Bisswanger81: Bisswanger H (1981). "Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli." J Biol Chem 256(2);815-22. PMID: 7005225

Dobson08: Dobson RC, Griffin MD, Devenish SR, Pearce FG, Hutton CA, Gerrard JA, Jameson GB, Perugini MA (2008). "Conserved main-chain peptide distortions: a proposed role for Ile203 in catalysis by dihydrodipicolinate synthase." Protein Sci 17(12);2080-90. PMID: 18787203

Lawrence97: Lawrence MC, Barbosa JA, Smith BJ, Hall NE, Pilling PA, Ooi HC, Marcuccio SM (1997). "Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase." J Mol Biol 266(2);381-99. PMID: 9047371

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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 19.0 on Tue Oct 13, 2015, biocyc13.