2-dehydro-3-deoxyglucarate aldolase
2-dehydro-3-deoxyglucarate aldolase | |||||||||
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![]() 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 | ||||||||
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In enzymology, a 2-dehydro-3-deoxyglucarate aldolase (EC 4.1.2.20) is an enzyme that catalyzes the chemical reaction
- 2-dehydro-3-deoxy-D-glucarate pyruvate + tartronate semialdehyde
Hence, this enzyme has one substrate, 2-dehydro-3-deoxy-D-glucarate, and two products, pyruvate and 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.