The enzyme phenylserine aldolase (EC 4.1.2.26) catalyzes the chemical reaction
| phenylserine aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.2.26 | ||||||||
| CAS no. | 37290-60-1 | ||||||||
| 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 | ||||||||
| |||||||||
- L-threo-3-phenylserine glycine + benzaldehyde
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 L-threo-3-phenylserine benzaldehyde-lyase (glycine-forming). This enzyme is also called L-threo-3-phenylserine benzaldehyde-lyase. It employs one cofactor, pyridoxal phosphate.
Structural studies edit
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1V72.
References edit
- BRUNS FH, FIEDLER L (1958). "Enzymatic cleavage and synthesis of L-threo-beta-phenylserine and L-erythro-beta-Phenyldrine". Nature. 181 (4622): 1533–4. Bibcode:1958Natur.181.1533B. doi:10.1038/1811533a0. PMID 13566053. S2CID 4277787.
