2-dehydro-3-deoxyglucarate aldolase
| 2-dehydro-3-deoxyglucarate aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
![]() 2-dehydro-3-deoxyglucarate aldolase hexamer, Staphylococcus aureus | |||||||||
| Identifiers | |||||||||
| EC no. | 4.1.2.20 | ||||||||
| CAS no. | 37290-56-5 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme 2-dehydro-3-deoxyglucarate aldolase (EC 4.1.2.20) catalyzes the chemical reaction
- 2-dehydro-3-deoxy-D-glucarate pyruvate + tartronate semialdehyde
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase (pyruvate-forming). Other names in common use include 2-keto-3-deoxyglucarate aldolase, alpha-keto-beta-deoxy-D-glucarate aldolase, and 2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase. This enzyme participates in ascorbate and aldarate metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1DXE, 1DXF, 1W37, 1W3I, 1W3N, and 1W3T.
References
- Fish DC, Blumenthal HJ (1966). "2-Keto-3-deoxy-D-glucarate aldolase". Carbohydrate Metabolism. Methods in Enzymology. Vol. 9. pp. 529–534. doi:10.1016/0076-6879(66)09105-5. ISBN 978-0-12-181809-8.
