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Literature summary extracted from

  • Wallner, S.; Winkler, A.; Riedl, S.; Dully, C.; Horvath, S.; Gruber, K.; Macheroux, P.
    Catalytic and structural role of a conserved active site histidine in berberine bridge enzyme (2012), Biochemistry, 51, 6139-6147.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.21.3.3 expression in Pichia pastoris Eschscholzia californica

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.21.3.3 crystal structure of the H174A variant shows significant structural rearrangements compared to wild-type enzyme. Residue H174 is part of a hydrogen bonding network that stabilizes the negative charge at the N1/C2=O locus via interaction with the hydroxyl group at C2 of the ribityl side chain of the flavin cofactor Eschscholzia californica

Protein Variants

EC Number Protein Variants Comment Organism
1.21.3.3 H174A mutation leads to substantial changes in all kinetic parameters and a decrease in midpoint potential. The crystal structure of the variant shows significant structural rearrangements compared to wild-type enzyme Eschscholzia californica

Organism

EC Number Organism UniProt Comment Textmining
1.21.3.3 Eschscholzia californica P30986
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Synonyms

EC Number Synonyms Comment Organism
1.21.3.3 berberine bridge-forming enzyme
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 Eschscholzia californica