Coniferyl-alcohol dehydrogenase
| coniferyl-alcohol dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.194 | ||||||||
| CAS no. | 37250-27-4 | ||||||||
| 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-alcohol dehydrogenase (EC 1.1.1.194) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are coniferyl alcohol and oxidised nicotinamide adenine dinucleotide phosphate (NADP+). Its products are coniferyl aldehyde, reduced NADPH, and a proton.[1][2][3]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is coniferyl-alcohol:NADP+ oxidoreductase. This enzyme is also called CAD.
References
- ^ Enzyme 1.1.1.194 at KEGG Pathway Database.
- ^ Mansell RL, Babbel GR, Zenk MH (1976). "Multiple forms and specificity of coniferyl alcohol dehydrogenase from cambial regions of higher plants". Phytochemistry. 15 (12): 1849–1853. Bibcode:1976PChem..15.1849M. doi:10.1016/S0031-9422(00)88829-9.
- ^ Wyrambik D, Grisebach H (1975). "Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures". Eur. J. Biochem. 59 (1): 9–15. doi:10.1111/j.1432-1033.1975.tb02418.x. PMID 1250.