Cinnamyl-alcohol dehydrogenase

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cinnamyl-alcohol dehydrogenase
Identifiers
EC no. 1.1.1.195
CAS no. 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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PMC articles
PubMed articles
NCBI proteins

In enzymology, cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) is an enzyme that catalyzes the chemical reaction

 
 
 
H+
Cinnamyl-alcohol dehydrogenase
 
H+
 
 

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

  1. Enzyme 1.1.1.195 at KEGG Pathway Database.
  2. 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.
  3. 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.
  4. Wyrambik D, Grisebach H (1979). "Enzymic synthesis of lignin precursors. Further studies on cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures". Eur. J. Biochem. 97 (2): 503–9. doi: 10.1111/j.1432-1033.1979.tb13138.x . PMID   572771.