3-hydroxyaspartate aldolase
The enzyme L-erythro-3-hydroxyaspartate aldolase (EC 4.1.3.14) catalyzes the chemical reaction
- L-erythro-3-hydroxy-aspartate glycine + glyoxylate
| L-erythro-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 | ||||||||
| |||||||||
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 L-erythro-3-hydroxy-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.
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