EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.19.51 | expression in Saccharomyces cerevisiae | Coptis japonica |
2.1.1.140 | expressed in Escherichia coli, recombinant CNMT protein | Coptis japonica |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.19.51 | microsome | sequence contains a putative endoplasmic reticulum-localizing signal | Coptis japonica | - |
- |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.19.51 | (S)-reticuline + [reduced NADPH-hemoprotein reductase] + O2 | Coptis japonica | - |
(S)-corytuberine + [oxidized NADPH-hemoprotein reductase] + 2 H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.19.51 | Coptis japonica | A8CDR5 | - |
- |
2.1.1.140 | Coptis japonica | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.19.51 | cell culture | - |
Coptis japonica | - |
2.1.1.140 | cell culture | - |
Coptis japonica | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.1.1.140 | additional information | - |
(S)-corytuberine conversion to magnoflorine shown by crude enzyme preparation of recombinant CNMT protein, magnoflorine biosynthesis by CYP80G2 protein and CjCNMT via (S)-corytuberine as an intermediate in vivo, CjCNMT protein catalyzes the crucial N-methylation step from (S)-coclaurine to (S)-N-methylcoclaurine in (S)-reticuline biosynthesis | Coptis japonica |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.19.51 | (R,S)-codamine + [reduced NADPH-hemoprotein reductase] + O2 | - |
Coptis japonica | 2,11-dimethoxy-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-1,10-diol + [oxidized NADPH-hemoprotein reductase] + 2 H2O | 12% of the activity with reticuline. The major product is (R,S)-orientaline, 4'-O-demethylation product of (R,S)-codamine, and the minor one is proposed to be the same compound as (R,S)-orientaline-derived phenol coupling product | ? | |
1.14.19.51 | (R,S)-norreticuline + [reduced NADPH-hemoprotein reductase] + O2 | - |
Coptis japonica | 2,10-dimethoxy-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-1,11-diol + [oxidized NADPH-hemoprotein reductase] + 2 H2O | 19% of the activity with reticuline | ? | |
1.14.19.51 | (S)-N-methylcoclaurine + [reduced NADPH-hemoprotein reductase] + O2 | - |
Coptis japonica | 2,11-dimethoxy-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-1,10-diol + [oxidized NADPH-hemoprotein reductase] + 2 H2O | 2% of the activity with reticuline | ? | |
1.14.19.51 | (S)-orientaline + [reduced NADPH-hemoprotein reductase] + O2 | - |
Coptis japonica | 2,11-dimethoxy-6-methyl-5,6,6a,7-tetrahydro-4H-dibenzo[de,g]quinoline-1,10-diol + [oxidized NADPH-hemoprotein reductase] + 2 H2O | 2.7% of the activity with reticuline | ? | |
1.14.19.51 | (S)-reticuline + [reduced NADPH-hemoprotein reductase] + O2 | - |
Coptis japonica | (S)-corytuberine + [oxidized NADPH-hemoprotein reductase] + 2 H2O | - |
? | |
1.14.19.51 | additional information | CC phenol-coupling reaction, requires NADPH and oxygen. The enzyme is specific for S-enantiomer of substrate | Coptis japonica | ? | - |
? | |
2.1.1.140 | additional information | involvement in magnoflorine biosynthesis determined, crude enzyme preparation of recombinant CNMT protein analyzed, recombinant CjCNMT protein shown to convert (S)-corytuberine to magnoflorine | Coptis japonica | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.19.51 | corytuberine synthase | - |
Coptis japonica |
1.14.19.51 | CYP80G2 | - |
Coptis japonica |
2.1.1.140 | CjCNMT | - |
Coptis japonica |
2.1.1.140 | CNMT protein | - |
Coptis japonica |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.19.51 | cytochrome P450 | - |
Coptis japonica |