Reaction participants Show >> << Hide
- Name help_outline (R)-N-methylcoclaurine Identifier CHEBI:57755 Charge 1 Formula C18H22NO3 InChIKeyhelp_outline BOKVLBSSPUTWLV-MRXNPFEDSA-O SMILEShelp_outline COc1cc2CC[NH+](C)[C@H](Cc3ccc(O)cc3)c2cc1O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (S)-N-methylcoclaurine Identifier CHEBI:57993 Charge 1 Formula C18H22NO3 InChIKeyhelp_outline BOKVLBSSPUTWLV-INIZCTEOSA-O SMILEShelp_outline COc1cc2CC[NH+](C)[C@@H](Cc3ccc(O)cc3)c2cc1O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,709 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
reduced [NADPH—hemoprotein reductase]
Identifier
RHEA-COMP:11964
Reactive part
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- Name help_outline FMNH2 Identifier CHEBI:57618 (Beilstein: 6258176) help_outline Charge -2 Formula C17H21N4O9P InChIKeyhelp_outline YTNIXZGTHTVJBW-SCRDCRAPSA-L SMILEShelp_outline Cc1cc2Nc3c([nH]c(=O)[nH]c3=O)N(C[C@H](O)[C@H](O)[C@H](O)COP([O-])([O-])=O)c2cc1C 2D coordinates Mol file for the small molecule Search links Involved in 794 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline berbamunine Identifier CHEBI:57894 Charge 2 Formula C36H42N2O6 InChIKeyhelp_outline FDABVSXGAMFQQH-XZWHSSHBSA-P SMILEShelp_outline COc1cc2CC[NH+](C)[C@@H](Cc3ccc(Oc4cc(C[C@H]5[NH+](C)CCc6cc(OC)c(O)cc56)ccc4O)cc3)c2cc1O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
oxidized [NADPH—hemoprotein reductase]
Identifier
RHEA-COMP:11965
Reactive part
help_outline
- Name help_outline FMN Identifier CHEBI:58210 Charge -3 Formula C17H18N4O9P InChIKeyhelp_outline ANKZYBDXHMZBDK-SCRDCRAPSA-K SMILEShelp_outline C12=NC([N-]C(C1=NC=3C(N2C[C@@H]([C@@H]([C@@H](COP(=O)([O-])[O-])O)O)O)=CC(=C(C3)C)C)=O)=O 2D coordinates Mol file for the small molecule Search links Involved in 804 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:23576 | RHEA:23577 | RHEA:23578 | RHEA:23579 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The purification and characterization of a unique cytochrome P-450 enzyme from Berberis stolonifera plant cell cultures.
Stadler R., Zenk M.H.
A new cytochrome P-450 enzyme, isolated from Berberis stolonifera plant cell suspension cultures, has been purified to electrophoretic homogeneity. The purified hemoprotein migrated as a single band in sodium dodecyl sulfate polyacrylamide gel electrophoresis with a minimal M(r) = 46,000. The enzy ... >> More
A new cytochrome P-450 enzyme, isolated from Berberis stolonifera plant cell suspension cultures, has been purified to electrophoretic homogeneity. The purified hemoprotein migrated as a single band in sodium dodecyl sulfate polyacrylamide gel electrophoresis with a minimal M(r) = 46,000. The enzyme could be purified to a high specific content of P-450 (18.2 nmol/mg protein) after fast protein liquid chromatofocusing, displaying an isoelectric point of 6.05. Spectral analysis of the homogeneous enzyme showed that it is predominantly low spin in the oxidized state, with a slight red-shifted ferrous carbonyl complex that exhibits a maximum at 452 nm. The purified cytochrome P-450, successfully reconstituted with NADPH-cytochrome P-450 reductase, displayed a maximal turnover rate of 50 nmol of substrate/nmol of P-450/min. In the purified and reconstituted form, the enzyme catalyzed the oxidation of three different chiral benzyltetrahydroisoquinoline substrates, namely (S)-coclaurine, (R)-N-methylcoclaurine, and (S)-N-methylcoclaurine, leading to the formation of three distinct dimeric products, (R,S)-berbamunine, (R,S)-2'-norberbamunine, and (R,R)-guattegaumerine, that are also present in the plant cell cultures in vivo. This is the first report of a P-450 enzyme that mediates regio- and stereoselective intermolecular oxidative phenol coupling to furnish natural dimeric compounds. In this catalytic cycle cytochrome P-450 functions as an oxidant in a bisubstrate reaction without transfer of the activated oxygen atom to either of the two chiral substrates. << Less