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Dihydrobenzophenanthridine oxidase (DHBP oxidase) is an enzyme. In the IUBMB Enzyme Nomenclature, dihydrobenzophenanthridine oxidase is EC 1.5.3.12.

Dihydrobenzophenanthridine oxidase produces oxidized forms of benzophenanthridine alkaloids:

In Sanguinaria canadensis (bloodroot), dihydrobenzophenanthridine oxidase produces sanguinarine from dihydrosanguinarine, and chelirubine from dihydrochelirubine.^[1]^[2]

dihydrosanguinarine

+ H₂O

O₂

H₂O₂

Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right

sanguinarine

+ H₂C=O

In Eschscholzia californica (California poppy), dihydrobenzophenanthridine oxidase produces macarpine from dihydromacarpine.^[3]

References

^ Rho D, Chauret N, Laberge N, Archambault J (1992). “Growth characteristics of Sanguinaria canadensis L. cell suspensions and immobilized cultures for production of benzophenanthridine alkaloids”. Appl. Microbiol. Biotechnol. 36 (5): 611–7. doi:10.1007/BF00183237. PMID 1368065.
^ Ignatov A, Clark WG, Cline SD, Psenak M, Krueger J, Coscia CJ (1996). “Elicitation of dihydrobenzophenanthridine oxidase in Sanguinaria canadensis cell cultures”. Phytochemistry. 43 (6): 1141–4. Bibcode:1996PChem..43.1141I. doi:10.1016/S0031-9422(96)00540-7. PMID 8987906.
^ Park SU, Yu M, Facchini PJ (2002). “Antisense RNA-mediated suppression of benzophenanthridine alkaloid biosynthesis in transgenic cell cultures of California poppy”. Plant Physiol. 128 (2): 696–706. doi:10.1104/pp.010741. PMC 148930. PMID 11842172.

External links

[rdp-we-cite_note-1] Rho D, Chauret N, Laberge N, Archambault J (1992). “Growth characteristics of Sanguinaria canadensis L. cell suspensions and immobilized cultures for production of benzophenanthridine alkaloids”. Appl. Microbiol. Biotechnol. 36 (5): 611–7. doi:10.1007/BF00183237. PMID 1368065.

[rdp-we-cite_note-2] Ignatov A, Clark WG, Cline SD, Psenak M, Krueger J, Coscia CJ (1996). “Elicitation of dihydrobenzophenanthridine oxidase in Sanguinaria canadensis cell cultures”. Phytochemistry. 43 (6): 1141–4. Bibcode:1996PChem..43.1141I. doi:10.1016/S0031-9422(96)00540-7. PMID 8987906.

[rdp-we-cite_note-3] Park SU, Yu M, Facchini PJ (2002). “Antisense RNA-mediated suppression of benzophenanthridine alkaloid biosynthesis in transgenic cell cultures of California poppy”. Plant Physiol. 128 (2): 696–706. doi:10.1104/pp.010741. PMC 148930. PMID 11842172.

[1]

[2]

[3]

Oxidoreductases: CH-NH (EC 1.5)
1.5.1: NAD or NADP acceptor	Dihydrofolate reductase Saccharopine dehydrogenase Methylenetetrahydrofolate reductase
1.5.3: oxygen acceptor	Dihydrobenzophenanthridine oxidase Sarcosine oxidase Proline oxidase
1.5.5: quinone acceptor	Electron-transferring-flavoprotein dehydrogenase
1.5.99	Sarcosine dehydrogenase Cytokinin dehydrogenase

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)