| perillyl-alcohol dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.144 | ||||||||
| CAS no. | 37250-73-0 | ||||||||
| 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, a perillyl-alcohol dehydrogenase ( EC 1.1.1.144) is an enzyme that catalyzes the chemical reaction
- perillyl alcohol + NAD+ perillyl aldehyde + NADH + H+
Thus, the two substrates of this enzyme are perillyl alcohol and NAD+, whereas its 3 products are perillyl aldehyde, NADH, and H+.
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 perillyl-alcohol:NAD+ oxidoreductase. This enzyme is also called perillyl alcohol dehydrogenase. This enzyme participates in limonene and pinene degradation.
References
- Ballal NR, Bhattacharyya PK, Rangachari PN (1966). "Perillyl alcohol dehydrogenase from a soil pseudomonad". Biochem. Biophys. Res. Commun. 23 (4): 473–8. doi: 10.1016/0006-291X(66)90752-2. PMID 4289759.
| perillyl-alcohol dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.144 | ||||||||
| CAS no. | 37250-73-0 | ||||||||
| 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, a perillyl-alcohol dehydrogenase ( EC 1.1.1.144) is an enzyme that catalyzes the chemical reaction
- perillyl alcohol + NAD+ perillyl aldehyde + NADH + H+
Thus, the two substrates of this enzyme are perillyl alcohol and NAD+, whereas its 3 products are perillyl aldehyde, NADH, and H+.
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 perillyl-alcohol:NAD+ oxidoreductase. This enzyme is also called perillyl alcohol dehydrogenase. This enzyme participates in limonene and pinene degradation.
References
- Ballal NR, Bhattacharyya PK, Rangachari PN (1966). "Perillyl alcohol dehydrogenase from a soil pseudomonad". Biochem. Biophys. Res. Commun. 23 (4): 473–8. doi: 10.1016/0006-291X(66)90752-2. PMID 4289759.