3-hydroxyaspartate aldolase
| 3-hydroxyaspartate aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.3.14 | ||||||||
| CAS no. | 37290-64-5 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a 3-hydroxyaspartate aldolase (EC 4.1.3.14) is an enzyme that catalyzes the chemical reaction
- erythro-3-hydroxy-Ls-aspartate glycine + glyoxylate
Hence, this enzyme has one substrate, , and two products, glycine and glyoxylate.
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is erythro-3-hydroxy-Ls-aspartate glyoxylate-lyase (glycine-forming). Other names in common use include erythro-beta-hydroxyaspartate aldolase, erythro-beta-hydroxyaspartate glycine-lyase, and erythro-3-hydroxy-Ls-aspartate glyoxylate-lyase.
References[]
- GIBBS RG, MORRIS JG (1964). "ASSAY AND PROPERTIES OF BETA-HYDROXYASPARTATE ALDOLASE FROM MICROCOCCUS DENITRIFICANS". Biochim. Biophys. Acta. 85: 501–3. doi:10.1016/0926-6569(64)90318-9. PMID 14194868.
Categories:
- EC 4.1.3
- Enzymes of unknown structure
- EC 4.1 stubs