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 | ||||||||
|
The enzyme benzoin aldolase ( EC 4.1.2.38) catalyzes the chemical reaction
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.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2AG0, 2AG1, and 2UZ1.
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 | ||||||||
|
The enzyme benzoin aldolase ( EC 4.1.2.38) catalyzes the chemical reaction
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.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2AG0, 2AG1, and 2UZ1.