Contains FAD. The enzyme, described from epiphytic marine bacteria of the genera Pseudoalteromonas and Marinomonas, is an unusual single-component FAD-dependent halogenase that contains a distinct NAD(P)H binding domain and does not require an additional flavin reductase for activity. The enzyme catalyses a bromination of its substrate, followed by a second bromination concurrent with decarboxylation.
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The enzyme appears in viruses and cellular organisms
Contains FAD. The enzyme, described from epiphytic marine bacteria of the genera Pseudoalteromonas and Marinomonas, is an unusual single-component FAD-dependent halogenase that contains a distinct NAD(P)H binding domain and does not require an additional flavin reductase for activity. The enzyme catalyses a bromination of its substrate, followed by a second bromination concurrent with decarboxylation.
coexpression of Bmp5 with flavin-dependent 4-hydroxybenzoate-3-hydroxylase m3553 in Escherichia coli yields 2,4-dibromophenol, 4-bromo-2-hydroxyphenol and 2,4-dibromo-6-hydroxyphenol. Coexpression of Bmp5, Cyp450 enzyme Bmp7, and m3553, and supplementation of the culture medium with exogenous 4-hydroxybenzoic acid, leads to production of bromophenols, bromocatechols, mono- and dihydroxylated dibenzo-p-dioxins, mono- and dihydroxy-brominated diphenyl ethers, as well as biphenyls
coexpression of Bmp5 with flavin-dependent 4-hydroxybenzoate-3-hydroxylase m3553 in Escherichia coli yields 2,4-dibromophenol, 4-bromo-2-hydroxyphenol and 2,4-dibromo-6-hydroxyphenol. Coexpression of Bmp5, Cyp450 enzyme Bmp7, and m3553, and supplementation of the culture medium with exogenous 4-hydroxybenzoic acid, leads to production of bromophenols, bromocatechols, mono- and dihydroxylated dibenzo-p-dioxins, mono- and dihydroxy-brominated diphenyl ethers, as well as biphenyls
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Enzyme Nomenclature
1.14.19.55 4-hydroxybenzoate brominase (decarboxylating)
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