EC Number | Cloned (Comment) | Organism |
---|---|---|
1.21.3.3 | expression in Pichia pastoris strain KM71H | Eschscholzia californica |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.21.3.3 | C166A | site-directed mutagenesis, the mutant protein still has residual activity, but reduced to about 6% of the turnover rate observed for wild-type berberine bridge enzyme, the reductive half-reaction is greatly influenced by the lack of the 6-S-cysteinyl linkage, resulting in a 370fold decrease in the rate of flavin reduction | Eschscholzia californica |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.21.3.3 | additional information | - |
additional information | steady-state kinetic analysis, and redox potentials for both wild type and C166A mutant enzyme are +132 mV and +53 mV, respectively, rapid reaction stopped-flow experiments, overview | Eschscholzia californica |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.21.3.3 | (S)-reticuline + O2 | Eschscholzia californica | - |
(S)-scoulerine + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.21.3.3 | Eschscholzia californica | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.21.3.3 | (S)-reticuline + O2 | - |
Eschscholzia californica | (S)-scoulerine + H2O2 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.21.3.3 | BBE | - |
Eschscholzia californica |
1.21.3.3 | berberine bridge enzyme | - |
Eschscholzia californica |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.21.3.3 | 37 | - |
assay at | Eschscholzia californica |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.21.3.3 | 0.48 | - |
(S)-reticuline | pH 9.0, 37°C, recombinant mutant C166A | Eschscholzia californica | |
1.21.3.3 | 103 | - |
(S)-reticuline | pH 9.0, 37°C, recombinant wild-type enzyme | Eschscholzia californica |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.21.3.3 | 9 | - |
assay at | Eschscholzia californica |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.21.3.3 | FAD | residues His104 and Cys166, which are involved in the bi-covalent attachment of FAD to berberine bridge enzyme | Eschscholzia californica |