Mannonate dehydratase
| mannonate dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.1.8 | ||||||||
| CAS no. | 9024-31-1 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a mannonate dehydratase (EC 4.2.1.8) is an enzyme that catalyzes the chemical reaction
- D-mannonate 2-dehydro-3-deoxy-D-gluconate + H2O
Hence, this enzyme has one substrate, D-mannonate, and two products, 2-dehydro-3-deoxy-D-gluconate 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 D-mannonate hydro-lyase (2-dehydro-3-deoxy-D-gluconate-forming). Other names in common use include mannonic hydrolase, mannonate hydrolyase, altronic hydro-lyase, altronate hydrolase, D-mannonate hydrolyase, and D-mannonate hydro-lyase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1TZ9.
References
- ASHWELL A, WAHBA AJ, HICKMAN J (1958). "A new pathway of uronic acid metabolism". Biochim. Biophys. Acta. 30 (1): 186–7. doi:10.1016/0006-3002(58)90257-9. PMID 13584413.
- Robert-Baudouy JM, Stoeber FR (1973). "[Purification and properties of D-mannonate hydrolyase from Escherichia coli K12]". Biochim. Biophys. Acta. 309 (2): 473–85. doi:10.1016/0005-2744(73)90045-4. PMID 4581499.
