Cinnamoyl-CoA reductase
| cinnamoyl-CoA reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.2.1.44 | ||||||||
| CAS number | 59929-39-4 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a cinnamoyl-CoA reductase (EC 1.2.1.44) is an enzyme that catalyzes the chemical reaction
- cinnamaldehyde + CoA + NADP+ cinnamoyl-CoA + NADPH + H+
The 3 substrates of this enzyme are cinnamaldehyde, CoA, and NADP+, whereas its 3 products are cinnamoyl-CoA, NADPH, and H+.
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 cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating). Other names in common use include feruloyl-CoA reductase, cinnamoyl-coenzyme A reductase, ferulyl-CoA reductase, feruloyl coenzyme A reductase, p-hydroxycinnamoyl coenzyme A reductase, and cinnamoyl-CoA:NADPH reductase. This enzyme participates in phenylpropanoid biosynthesis.
References
- Gross GG, Kreiten W (1975). "Reduction of coenzyme A thioesters of cinnamic acids with an enzyme preparation from lignifying tissue of Forsythia". FEBS Lett. 54 (2): 259–62. doi:10.1016/0014-5793(75)80087-1. PMID 236926.
- Sarni F, Grand C, Boudet AM (1984). "Purification and properties of cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase from poplar stems (Populus X euramericana)". Eur. J. Biochem. 139 (2): 259–65. doi:10.1111/j.1432-1033.1984.tb08002.x. PMID 6365550.
- Wengenmayer H, Ebel J, Grisebach H (1976). "Enzymic synthesis of lignin precursors. Purification and properties of a cinnamoyl-CoA: NADPH reductase from cell suspension cultures of soybean (Glycinemax)". Eur. J. Biochem. 65 (2): 529–36. doi:10.1111/j.1432-1033.1976.tb10370.x. PMID 7454.