Trans-cinnamate 2-monooxygenase

Trans-cinnamate 2-monooxygenase
Identifiers
EC no.1.14.13.14
CAS no.53126-56-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Trans-cinnamate 2-monooxygenase (EC 1.14.13.14) is an enzyme that catalyzes the chemical reaction

 
 
O2 + H+
H2O
 
 
 
 

The four substrates of this enzyme are cinnamic acid, reduced nicotinamide adenine dinucleotide phosphate (NADPH), oxygen, and a proton. Its products are o-coumaric acid, oxidised NADP+, and water.[1][2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is trans-cinnamate,NADPH:oxygen oxidoreductase (2-hydroxylating). Other names in common use include cinnamic acid 2-hydroxylase, cinnamate 2-monooxygenase, cinnamic 2-hydroxylase, cinnamate 2-hydroxylase, and trans-cinnamic acid 2-hydroxylase. This enzyme participates in phenylalanine metabolism and phenylpropanoid biosynthesis.

References

  1. ^ Enzyme 1.14.13.14 at KEGG Pathway Database.
  2. ^ Gestetner B, Conn EE (1974). "The 2-hydroxylation of trans-cinnamic acid by chloroplasts from Melilotus alba Desr". Arch. Biochem. Biophys. 163 (2): 617–24. doi:10.1016/0003-9861(74)90522-0. PMID 4153528.