Categories
Cinnamyl-alcohol dehydrogenase
Topic: Biology
From HandWiki - Reading time: 4 min
| cinnamyl-alcohol dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.195 | ||||||||
| CAS number | 55467-36-2 | ||||||||
| 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 | ||||||||
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In enzymology, cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are cinnamyl alcohol and oxidised nicotinamide adenine dinucleotide phosphate (NADP+). Its products are cinnamaldehyde, reduced NADPH, and a proton.[1][2][3][4]
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 cinnamyl-alcohol:NADP+ oxidoreductase. Other names in common use include cinnamyl alcohol dehydrogenase, and CAD. This enzyme participates in phenylpropanoid biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1YQD, 1YQX, 2CF5, and 2CF6.
References
- ↑ Enzyme 1.1.1.195 at KEGG Pathway Database.
- ↑ "Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase from poplar stems (Populus X euramericana)". Eur. J. Biochem. 139 (2): 259–65. 1984. doi:10.1111/j.1432-1033.1984.tb08002.x. PMID 6365550.
- ↑ "Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures". Eur. J. Biochem. 59 (1): 9–15. 1975. doi:10.1111/j.1432-1033.1975.tb02418.x. PMID 1250.
- ↑ "Enzymic synthesis of lignin precursors. Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures". Eur. J. Biochem. 97 (2): 503–9. 1979. doi:10.1111/j.1432-1033.1979.tb13138.x. PMID 572771.
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