Biology:D(−)-tartrate dehydratase
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Short description: Enzyme
D(−)-tartrate dehydratase | |||||||||
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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 / QuickGO | ||||||||
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The enzyme D(−)-tartrate dehydratase (EC 4.2.1.81) catalyzes the chemical reaction
- (S,S)-tartrate [math]\displaystyle{ \rightleftharpoons }[/math] oxaloacetate + 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
- "D-(--)-tartrate dehydratase of Rhodopseudomonas sphaeroides: purification, characterization, and application to enzymatic determination of D-(--)-tartrate". J. Bacteriol. 150 (3): 1061–8. 1982. doi:10.1128/JB.150.3.1061-1068.1982. PMID 6978882.
- "Ferrous- or cobalt ion-dependent D-(−)-tartrate dehydratase of pseudomonads: purification and properties". J. Bacteriol. 151 (3): 1602–4. 1982. doi:10.1128/JB.151.3.1602-1604.1982. PMID 7107563.
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