Phenylserine aldolase
| 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 | ||||||||
| |||||||||
In enzymology, a phenylserine aldolase (EC 4.1.2.26) is an enzyme that catalyzes the chemical reaction
- L-threo-3-phenylserine glycine + benzaldehyde
Hence, this enzyme has one substrate, L-threo-3-phenylserine, and two products, glycine and 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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1V72.
References
- BRUNS FH, FIEDLER L (1958). "Enzymatic cleavage and synthesis of L-threo-beta-phenylserine and L-erythro-beta-Phenyldrine". Nature. 181 (4622): 1533–4. doi:10.1038/1811533a0. PMID 13566053.
