| 2-dehydropantoate aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.2.12 | ||||||||
| CAS no. | 9024-51-5 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme 2-dehydropantoate aldolase ( EC 4.1.2.12) catalyzes the chemical reaction:
- 2-dehydropantoate 3-methyl-2-oxobutanoate + formaldehyde
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-dehydropantoate formaldehyde-lyase (3-methyl-2-oxobutanoate-forming). Other names in common use include ketopantoaldolase, and 2-dehydropantoate formaldehyde-lyase.
- McIntosh EN, Purko M, Wood WA (1957). "Ketopantoate formation by a hydroxymethylation enzyme from Escherichia coli". J. Biol. Chem. 228 (1): 499–510. PMID 13475336.
| 2-dehydropantoate aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.2.12 | ||||||||
| CAS no. | 9024-51-5 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme 2-dehydropantoate aldolase ( EC 4.1.2.12) catalyzes the chemical reaction:
- 2-dehydropantoate 3-methyl-2-oxobutanoate + formaldehyde
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-dehydropantoate formaldehyde-lyase (3-methyl-2-oxobutanoate-forming). Other names in common use include ketopantoaldolase, and 2-dehydropantoate formaldehyde-lyase.
- McIntosh EN, Purko M, Wood WA (1957). "Ketopantoate formation by a hydroxymethylation enzyme from Escherichia coli". J. Biol. Chem. 228 (1): 499–510. PMID 13475336.