Coniferyl-aldehyde dehydrogenase
| coniferyl-aldehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.68 | ||||||||
| 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, coniferyl-aldehyde dehydrogenase (EC 1.2.1.68) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are (E)-coniferyl aldehyde, oxidised nicotinamide adenine dinucleotide (NAD+), and water. Its products are ferulic acid, reduced NADH, and a proton. The enzyme can use nicotinamide adenine dinucleotide phosphate as an alternative cofactor.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coniferyl aldehyde:NAD(P)+ oxidoreductase.
References
- ^ Enzyme 1.2.1.68 at KEGG Pathway Database.
- ^ Achterholt S, Priefert H, Steinbuchel A (1998). "Purification and characterization of the coniferyl aldehyde dehydrogenase from Pseudomonas sp. Strain HR199 and molecular characterization of the gene". J. Bacteriol. 180 (17): 4387–91. doi:10.1128/JB.180.17.4387-4391.1998. PMC 107445. PMID 9721273.