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Literature summary for 1.3.1.107 extracted from

  • Vogel, M.; Lawson, M.; Sippl, W.; Conrad, U.; Roos, W.
    Structure and mechanism of sanguinarine reductase, an enzyme of alkaloid detoxification (2010), J. Biol. Chem., 285, 18397-18406.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in bacteria Eschscholzia californica

Crystallization (Commentary)

Crystallization (Comment) Organism
modeling of spatial conformation and catalytic site based on PDB entry 1XQ6 Eschscholzia californica

Protein Variants

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

Organism UniProt Comment Textmining
Eschscholzia californica D5JWB3
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Substrates and Products (Substrate)

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 ?
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