Benzoin aldolase
| benzoin aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.2.38 | ||||||||
| CAS no. | 122097-01-2 | ||||||||
| 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 benzoin aldolase (EC 4.1.2.38) is an enzyme that catalyzes the chemical reaction
- benzoin 2 benzaldehyde
Hence, this enzyme has one substrate, benzoin, and one product, 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 2-hydroxy-1,2-diphenylethanone benzaldehyde-lyase (benzaldehyde-forming)—the systematic name of benzoin is 2-hydroxy-1,2-diphenylethanone. Other names in common use include benzaldehyde lyase, and 2-hydroxy-1,2-diphenylethanone benzaldehyde-lyase. It employs one cofactor, thiamin diphosphate.
Structural studies[]
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2AG0, 2AG1, and 2UZ1.
References[]
- Gonzalez B, Vicuna R (1989). "Benzaldehyde lyase, a novel thiamine PPi-requiring enzyme, from Pseudomonas fluorescens biovar I". J. Bacteriol. 171 (5): 2401–5. doi:10.1128/jb.171.5.2401-2405.1989. PMC 209914. PMID 2496105.
- Peng M, Siebert D, Engqvist M, Niemeyer C, Rabe K (2021). "Modeling-Assisted Design of Thermostable Benzaldehyde Lyases from Rhodococcus erythropolis for Continuous Production of α-Hydroxy Ketones". ChemBioChem. doi:10.1002/cbic.202100468. PMID 2496105.
- EC 4.1.2
- Thiamine enzymes
- Enzymes of known structure
- EC 4.1 stubs