Literature summary for 1.21.3.3 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Pichia pastoris	Eschscholzia californica

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Eschscholzia californica	P30986	-	-

Synonyms

Synonyms	Comment	Organism
berberine bridge-forming enzyme	-	Eschscholzia californica

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Release 2023.1 (January 2023)