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1.21.3.3: reticuline oxidase

This is an abbreviated version!
For detailed information about reticuline oxidase, go to the full flat file.

Word Map on EC 1.21.3.3

Reaction

(S)-reticuline
+
O2
=
(S)-scoulerine
 +
H2O2

Synonyms

(S)-reticuline oxidase, BBE, BBE-like 13, BBE-like 15, BBE-like 28, BBE1, BBL, berberine bridge enzyme, berberine bridge enzyme-like, berberine bridge enzyme-like 28, berberine bridge-forming enzyme, berberine-bridge-forming enzyme, EC 1.5.3.9, flavin-dependent oxidase, monolignol oxidoreductase, reticuline oxidase, tetrahydroprotoberberine synthase

ECTree

     1 Oxidoreductases
         1.21 Catalysing the reaction X-H + Y-H = X-Y
             1.21.3 With oxygen as acceptor
                1.21.3.3 reticuline oxidase

Crystallization

Crystallization on EC 1.21.3.3 - reticuline oxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.2 M sodium thiocyanate and 20% (w/v) PEG 3350
microbatch method, using 0.1 M HEPES buffer pH 7.0 containing 30% (v/v) Jeffamine ED 2001, pH 7.0
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
the crystal structure of Berberine bridge enzyme in complex with dehydroscoulerine is determined to 1.63 A resolution
the crystal structures of berberine bridge enzyme in two different crystal forms, monoclinic and tetragonal, and in complex with (S)-reticuline are determined
-
the crystal structures of the mutants H104A, C166A, C166A in complex with (S)-reticuline and of the wild-type enzyme in complex with (S)-scoulerine are determined