Some oxygen-dependent oxidoreductases are flavoproteins that contains a
covalently bound FAD group which is attached to a histidine via an 8-α-(N3-histidyl)-riboflavin linkage. These proteins are:
(R)-6-hydroxynicotine oxidase (EC 1.5.3.6) (6-HDNO) [1], a bacterial enzyme
that catalyzes the oxygen-dependent degradation of 6-hydroxynicotine into
6-hydroxypyrid-N-methylosmine.
Plant reticuline oxidase (EC 1.21.3.3) [2] (berberine-bridge-forming
enzyme), an enzyme that catalyzes the oxidation of (S)-reticuline into (S)-
scoulerine in the pathway leading to benzophenanthridine alkaloids.
L-gulonolactone oxidase (EC 1.1.3.8) (l-gulono-γ-lactone oxidase) [3],
a mammalian enzyme which catalyzes the oxidation of L-gulono-1,4-lactone to
L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
D-arabinono-1,4-lactone oxidase (EC 1.1.3.24) (L-galactonolactone oxidase),
a yeast enzyme involved in the biosynthesis of D-erythroascorbic acid [4].
Mitomycin radical oxidase [5], a bacterial protein involved in mitomycin
resistance and that probably oxidizes the reduced form of mitomycins.
Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack.
Isolation and sequence analysis of a complementary DNA encoding rat liver L-gulono-gamma-lactone oxidase, a key enzyme for L-ascorbic acid biosynthesis.
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