Enzymes
| UniProtKB help_outline | 11,259 proteins |
| Enzyme class help_outline |
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| GO Molecular Function help_outline |
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- Name help_outline (2R,3R)-tartrate Identifier CHEBI:30924 (Beilstein: 3906378; CAS: 87-69-4) help_outline Charge -2 Formula C4H4O6 InChIKeyhelp_outline FEWJPZIEWOKRBE-JCYAYHJZSA-L SMILEShelp_outline O[C@H]([C@@H](O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline oxaloacetate Identifier CHEBI:16452 (CAS: 149-63-3) help_outline Charge -2 Formula C4H2O5 InChIKeyhelp_outline KHPXUQMNIQBQEV-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 60 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:15413 | RHEA:15414 | RHEA:15415 | RHEA:15416 | |
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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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Identification of the L-tartrate dehydratase genes (ttdA and ttdB) of Escherichia coli and evolutionary relationship with the class I fumarase genes.
Reaney S.K., Begg C., Bungard S.I., Guest J.R.
The genes encoding an oxygen-labile stereospecific L-tartrate dehydratase (L-Ttd, EC 4.2.1.32) have been identified as the orfZ1 and orfZ2 genes located upstream of the rpsU-dnaG-rpoD operon at 67 min in the Escherichia coli linkage map. They were previously cloned and sequenced by M. Nesin and ot ... >> More
The genes encoding an oxygen-labile stereospecific L-tartrate dehydratase (L-Ttd, EC 4.2.1.32) have been identified as the orfZ1 and orfZ2 genes located upstream of the rpsU-dnaG-rpoD operon at 67 min in the Escherichia coli linkage map. They were previously cloned and sequenced by M. Nesin and others (Gene 51, 149-161, 1987) and have now been independently cloned, partially resequenced, and designated as an operon (ttdAB) containing two translationally coupled genes. The enzyme behaves as a tetramer (M(r) 105,000) containing two pairs of non-identical subunits, TtdA (M(r) 32589) and TtdB (M(r) 22641), which otherwise resembles the homodimeric iron-sulphur-containing Class I fumarases of E. coli and Bacillus stearothermophilus. The amino acid sequences of the TtdA-TtdB subunits are colinearly related to a single fumarase subunit, indicating a common evolutionary ancestry. E. coli can use L-, D- and meso-tartrates as aerobic growth substrates and as reducible substrates for supporting anaerobic growth on glycerol. L-Ttd was induced during anaerobic growth on glycerol plus L- and meso-tartrates, and a stereospecific D-tartrate dehydratase was induced by all three stereoisomers under comparable conditions. No meso-tartrate dehydratase was detected, nor were any dehydratases detected after aerobic growth on tartrate minimal media suggesting that different catabolic routes operate under aerobic conditions. << Less
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TARTARIC ACID METABOLISM. I. SUBUNITS OF L(+)-TARTARIC ACID DEHYDRASE.
HURLBERT R.E., JAKOBY W.B.