D(-)-tartrate dehydratase
| D(−)-tartrate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.1.81 | ||||||||
| CAS number | 82532-88-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a D(−)-tartrate dehydratase (EC 4.2.1.81) is an enzyme that catalyzes the chemical reaction
- (S,S)-tartrate oxaloacetate + H2O
Hence, this enzyme has one substrate, (S,S)-tartrate, and two products, oxaloacetate and H2O.
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (S,S)-tartrate hydro-lyase (oxaloacetate-forming). Other names in common use include D-tartrate dehydratase, and (S,S)-tartrate hydro-lyase. It has 2 cofactors: iron, and Manganese.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2DW6 and 2DW7.
References
- Rode H, Giffhorn F (1982). "D-(--)-tartrate dehydratase of Rhodopseudomonas sphaeroides: purification, characterization, and application to enzymatic determination of D-(--)-tartrate". J. Bacteriol. 150 (3): 1061–8. PMC 216323
. PMID 6978882. - Rode H, Giffhorn F (1982). "Ferrous- or cobalt ion-dependent D-(−)-tartrate dehydratase of pseudomonads: purification and properties". J. Bacteriol. 151 (3): 1602–4. PMC 220444. PMID 7107563.
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