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- Name help_outline 3-hydroxypyruvate Identifier CHEBI:17180 Charge -1 Formula C3H3O4 InChIKeyhelp_outline HHDDCCUIIUWNGJ-UHFFFAOYSA-M SMILEShelp_outline OCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 21 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-hydroxy-3-oxopropanoate Identifier CHEBI:57978 Charge -1 Formula C3H3O4 InChIKeyhelp_outline QWBAFPFNGRFSFB-UHFFFAOYSA-M SMILEShelp_outline [H]C(=O)C(O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:11952 | RHEA:11953 | RHEA:11954 | RHEA:11955 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Biochemical evidence that Escherichia coli hyi (orf b0508, gip) gene encodes hydroxypyruvate isomerase.
Ashiuchi M., Misono H.
We found a significant activity of hydroxypyruvate isomerase in Escherichia coli clone cells harboring an E. coli gene (called orf b0508 or gip), which is located downstream of the glyoxylate carboligase gene. We newly designated the gene hyi. The enzyme was purified from cell extracts of the E. c ... >> More
We found a significant activity of hydroxypyruvate isomerase in Escherichia coli clone cells harboring an E. coli gene (called orf b0508 or gip), which is located downstream of the glyoxylate carboligase gene. We newly designated the gene hyi. The enzyme was purified from cell extracts of the E. coli clone. The enzyme had a molecular mass of 58 kDa and was composed of two identical subunits. The optimum pH for the isomerization of hydroxypyruvate was 6.8-7.2. The enzyme required no cofactor. It exclusively catalyzed the isomerization between hydroxypyruvate and tartronate semialdehyde. The apparent K(m) value for hydroxypyruvate was 12.5 mM. The amino acid sequence of E. coli hydroxypyruvate isomerase is highly similar to those of glyoxylate-induced proteins, Gip, found widely from prokaryotes to eukaryotes. << Less
Biochim. Biophys. Acta 1435:153-159(1999) [PubMed] [EuropePMC]
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Purification and some properties of hydroxypyruvate isomerase of Bacillus fastidiosus.
de Windt F.E., van der Drift C.
Hydroxypyruvate isomerase of Bacillus fastidiosus is a novel enzyme (Braun, W. and Kaltwasser, H. (1979) Arch. Microbiol. 121, 129-134) which catalyzes the reversible conversion of tartronate semialdehyde into hydroxypyruvate. The enzyme was purified to homogeneity. The native molecule had a molec ... >> More
Hydroxypyruvate isomerase of Bacillus fastidiosus is a novel enzyme (Braun, W. and Kaltwasser, H. (1979) Arch. Microbiol. 121, 129-134) which catalyzes the reversible conversion of tartronate semialdehyde into hydroxypyruvate. The enzyme was purified to homogeneity. The native molecule had a molecular weight of 265 000-280 000 and was composed of six subunits with a molecular weight of 45 000. The enzyme showed optimal activity at pH 6.6-7.4 and 57 degrees C. Hydroxypyruvate isomerase is stable on heating for 10 min at 67 degrees C. The enzyme appeared to be specific for tartronate semialdehyde and hydroxypyyruvate and no cofactors were involved in the reaction. The equilibrium constant K = [tartronate semialdehyde] divided by [hydroxypyruvate] was found to be 2.5 at pH 7.1, and 30 degrees C. << Less