Cloned (Comment) | Organism |
---|---|
expression in bacteria | Eschscholzia californica |
Crystallization (Comment) | Organism |
---|---|
modeling of spatial conformation and catalytic site based on PDB entry 1XQ6 | Eschscholzia californica |
Protein Variants | Comment | Organism |
---|---|---|
C157A | 15.1% of wild-type activity | Eschscholzia californica |
D158N | 47.1% of wild-type activity | Eschscholzia californica |
DELTA102-114 | 2.5% of wild-type activity | Eschscholzia californica |
F162P | 22% of wild-type activity | Eschscholzia californica |
H161A | 15.6% of wild-type activity | Eschscholzia californica |
M166L | 64.5% of wild-type activity | Eschscholzia californica |
S153A | 4.0% of wild-type activity | Eschscholzia californica |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Eschscholzia californica | D5JWB3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | catalytic mechanism is as follows: the alkanolamine form of sanguinarine is fixed in a binding pocket, mainly consisting of hydrophobic amino acids, by the conserved residue Ser153. Both dioxolane rings of the alkaloid are bound by a triad of H-bonds originating from Cys157 connected to Asp158 and His161 and by the side chain of Lys175. Electron transfer is initiated by attacking the C6 of sanguinarine with the hydride ion of NADPH and the OH group at C6 with a proton originating from Ser153. The anionic form of Ser is then stabilized by the NH3+ group of Lys175. Removal of OH- followed by water formation completes the reduction process | Eschscholzia californica | ? | - |
? |