Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.21.3.3 extracted from

  • Winkler, A.; Kutchan, T.M.; Macheroux, P.
    6-S-cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity (2007), J. Biol. Chem., 282, 24437-24443.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris strain KM71H Eschscholzia californica

Protein Variants

Protein Variants Comment Organism
C166A site-directed mutagenesis, the mutant protein still has residual activity, but reduced to about 6% of the turnover rate observed for wild-type berberine bridge enzyme, the reductive half-reaction is greatly influenced by the lack of the 6-S-cysteinyl linkage, resulting in a 370fold decrease in the rate of flavin reduction Eschscholzia californica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic analysis, and redox potentials for both wild type and C166A mutant enzyme are +132 mV and +53 mV, respectively, rapid reaction stopped-flow experiments, overview Eschscholzia californica

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Eschscholzia californica
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
BBE
-
Eschscholzia californica
berberine bridge enzyme
-
Eschscholzia californica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Eschscholzia californica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.48
-
(S)-reticuline pH 9.0, 37°C, recombinant mutant C166A Eschscholzia californica
103
-
(S)-reticuline pH 9.0, 37°C, recombinant wild-type enzyme Eschscholzia californica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Eschscholzia californica

Cofactor

Cofactor Comment Organism Structure
FAD residues His104 and Cys166, which are involved in the bi-covalent attachment of FAD to berberine bridge enzyme Eschscholzia californica