Propanediol dehydratase
In enzymology, a propanediol dehydratase (EC 4.2.1.28) is an enzyme that catalyzes the chemical reaction
- propane-1,2-diol propanal + H2O
| propanediol dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.1.28 | ||||||||
| CAS number | 9026-90-8 | ||||||||
| 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 | ||||||||
| |||||||||
Hence, this enzyme has one substrate, 1,2-propanediol, and two products, propanal 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 propane-1,2-diol hydro-lyase (propanal-forming). Other names in common use include meso-2,3-butanediol dehydrase, diol dehydratase, DL-1,2-propanediol hydro-lyase, diol dehydrase, adenosylcobalamin-dependent diol dehydratase, propanediol dehydrase, coenzyme B12-dependent diol dehydrase, 1,2-propanediol dehydratase, dioldehydratase, and propane-1,2-diol hydro-lyase. This enzyme participates in glycerolipid metabolism. It employs one cofactor, cobamide.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1DIO, 1EEX, 1EGM, 1EGV, 1IWB, 1UC4, and 1UC5.
References
- ABELES RH, LEE HA (1961). "An intramolecular oxidation-reduction requiring a cobamide coenzyme". J. Biol. Chem. 236: 2347–50. PMID 13680987.
- Forage RG, Foster MA (1982). "Glycerol fermentation in Klebsiella pneumoniae: functions of the coenzyme B12-dependent glycerol and diol dehydratases". J. Bacteriol. 149 (2): 413–9. doi:10.1128/JB.149.2.413-419.1982. PMC 216523. PMID 7035429.
- LEE HA, ABELES RH (1963). "Purification and properties of dioldehydrase, and enzyme requiring a cobamide coenzyme". J. Biol. Chem. 238: 2367–73. PMID 13929077.