(S)-Tetrahydroberberine oxidase (EC 1.3.3.8) is an enzyme that catalyzes the final transformation in the biosynthesis of berberine, a quaternary benzylisoquinoline alkaloid of the protoberberine structural subgroup.[1][2] This reaction pathway catalyzes the four-electron oxidation of (S)-tetrahydroberberine (also known as (S)-canadine) in the presence of oxygen to produce berberine and hydrogen peroxide as products.
| tetrahydroberberine oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.3.8 | ||||||||
| CAS no. | 114705-00-9 | ||||||||
| 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 | ||||||||
| |||||||||
(S)-Tetrahydroberberine 2 O2 ⇌ Berberine 2 H2O2
This enzyme belongs to the family known as oxidoreductases, in this instance the CH-CH moiety acts as the electron donor with oxygen acting as the electron acceptor. The systematic name of this enzyme is (S)-tetrahydroberberine:oxygen oxidoreductase; but it is also known as (S)-THB oxidase, tetrahydroberberine oxidase, and decreasingly, as (S)-tetrahydroprotoberberine oxidase.[3][4]
References
edit- ^ Amann M, Nagakura N, Zenk MH (July 1988). "Purification and properties of (S)-tetrahydroprotoberberine oxidase from suspension-cultured cells of Berberis wilsoniae". European Journal of Biochemistry. 175 (1): 17–25. doi:10.1111/j.1432-1033.1988.tb14160.x. PMID 3402447.17-25&rft.date=1988-07&rft_id=info:doi/10.1111/j.1432-1033.1988.tb14160.x&rft_id=info:pmid/3402447&rft.aulast=Amann&rft.aufirst=M&rft.au=Nagakura, N&rft.au=Zenk, MH&rft_id=https://doi.org/10.1111%2Fj.1432-1033.1988.tb14160.x&rfr_id=info:sid/en.wikipedia.org:Tetrahydroberberine oxidase" class="Z3988">
- ^ Amann M, Nagakura N, Zenk MH (1984). "(S)-tetrahydroprotoberberine oxidase the final enzyme in protoberberine biosynthesis". Tetrahedron Lett. 25 (9): 953–4. doi:10.1016/S0040-4039(01)80071-X.953-4&rft.date=1984&rft_id=info:doi/10.1016/S0040-4039(01)80071-X&rft.aulast=Amann&rft.aufirst=M&rft.au=Nagakura, N&rft.au=Zenk, MH&rfr_id=info:sid/en.wikipedia.org:Tetrahydroberberine oxidase" class="Z3988">
- ^ Okada N, Shinmyo A, Okada H, Yamada Y (1988). "Purification and characterization of (S)-tetrahydroberberine oxidase from cultured Coptis japonica cells". Phytochemistry. 27 (4): 979–82. doi:10.1016/0031-9422(88)80255-3.979-82&rft.date=1988&rft_id=info:doi/10.1016/0031-9422(88)80255-3&rft.aulast=Okada&rft.aufirst=N&rft.au=Shinmyo, A&rft.au=Okada, H&rft.au=Yamada, Y&rfr_id=info:sid/en.wikipedia.org:Tetrahydroberberine oxidase" class="Z3988">
- ^ Okada N, Koizumi N, Tanaka T, Ohkubo H, Nakanishi S, Yamada Y (January 1989). "Isolation, sequence, and bacterial expression of a cDNA for (S)-tetrahydroberberine oxidase from cultured berberine-producing Coptis japonica cells". Proceedings of the National Academy of Sciences of the United States of America. 86 (2): 534–8. Bibcode:1989PNAS...86..534O. doi:10.1073/pnas.86.2.534. PMC 286506. PMID 2463630.534-8&rft.date=1989-01&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC286506#id-name=PMC&rft_id=info:pmid/2463630&rft_id=info:doi/10.1073/pnas.86.2.534&rft_id=info:bibcode/1989PNAS...86..534O&rft.aulast=Okada&rft.aufirst=N&rft.au=Koizumi, N&rft.au=Tanaka, T&rft.au=Ohkubo, H&rft.au=Nakanishi, S&rft.au=Yamada, Y&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC286506&rfr_id=info:sid/en.wikipedia.org:Tetrahydroberberine oxidase" class="Z3988">
