Literature summary for 1.21.3.3 extracted from

Winkler, A.; Hartner, F.; Kutchan, T.M.; Glieder, A.; Macheroux, P.
Biochemical evidence that berberine bridge enzyme belongs to a novel family of flavoproteins containing a bi-covalently attached FAD cofactor (2006), J. Biol. Chem., 281, 21276-21285.

Search for more literature for 1.21.3.3

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
59599	-	x * 59599, calculated, including FAD cofactor	Eschscholzia californica

Organism

Organism	UniProt	Comment	Textmining
Eschscholzia californica	-	expression in Pichia pastoris	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	three potential N-glycosylation sites, one at the N-terminus, N38, and two at the C-terminus, Asn-423 and Asn-471	Eschscholzia californica

Source Tissue

Source Tissue	Comment	Organism	Textmining
culture fluid	recombinant enzyme	Eschscholzia californica	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-reticuline + O2	-	Eschscholzia californica	(S)-scoulerine + H2O2	-	?

Subunits

Subunits	Comment	Organism
?	x * 59599, calculated, including FAD cofactor	Eschscholzia californica

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
8.2	-	(S)-reticuline	pH 9.0, 37°C	Eschscholzia californica

Cofactor

Cofactor	Comment	Organism	Structure
FAD	covalently attached to enzyme at 8alpha position to H104 and also at 6 position to thiol group of C166. anaerobic photoirradiation leads to cleavage of the linkage to C166 yielding 6-mercaptoflavin and a peptide with C replaced by A due to breakage of the C-S bond	Eschscholzia californica

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Release 2023.1 (January 2023)