Reticuline oxidase

reticuline oxidase
Identifiers
EC no.1.21.3.3
CAS no.152232-28-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, reticuline oxidase (EC 1.21.3.3) is an enzyme that catalyzes the chemical reaction

 
O2
2 H2O
 
 
 

The two substrates of this enzyme are (S)-reticuline and oxygen. Its products are scoulerine and hydrogen peroxide.[1][2][3]

This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is (S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming). Other names in common use include BBE, berberine bridge enzyme, berberine-bridge-forming enzyme, and tetrahydroprotoberberine synthase. This enzyme participates in alkaloid biosynthesis.[4]

References

  1. ^ Enzyme 1.21.3.3 at KEGG Pathway Database.
  2. ^ Steffens P, Nagakura N, Zenk MH (1984). "The berberine bridge forming enzyme in tetrahydroprotoberberine biosynthesis". Tetrahedron Lett. 25 (9): 951–952. doi:10.1016/S0040-4039(01)80070-8.
  3. ^ Dittrich H, Kutchan TM (1991). "Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack". Proc. Natl. Acad. Sci. U.S.A. 88 (22): 9969–73. Bibcode:1991PNAS...88.9969D. doi:10.1073/pnas.88.22.9969. PMC 52848. PMID 1946465.
  4. ^ Kutchan TM, Dittrich H (1995). "Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in plants". J. Biol. Chem. 270 (41): 24475–81. doi:10.1074/jbc.270.41.24475. PMID 7592663.