The biosynthesis of pentabromopseudilin, among other halopyrroles, has been elucidated via the identification of the conserved brominated marine pyrroles/phenols (bmp) pathway first identified in the marine bacteria, P. luteoviolacea 2ta16 and P. phenolica O-BC30.
The bmp pathway describes a bi-modular scheme for polybrominated marine microbial natural products production.
In the first module, the bromophenol moiety of PBP is first assembled from a chorismate precursor which is then converted by Bmp6, a chorismate lyase (CL), to yield 4-HBA.
4-HBA is then di-halogenated by the flavin-dependent halogenase, Bmp5 (Hal), to yield 2,3-dibromophenol.

Consistent with earlier isotopic studies, the PBP halopyrrole biosynthesis via the bmp pathway begins with L-proline.
In this module, L-proline is acylated to the acyl carrier protein domain of Bmp1 (ACP-thioesterase (TE) di-domain protein) by the proline adenyl transferase Bmp4 (A).
 The flavin-dependent dehydrogenase, Bmp3 (DH), then oxidizes the prolyl ring to a pyrrole.
The loaded protein is then tri-brominated with the flavin-dependent halogenase, Bmp2 (Hal), becoming 2,3,4,5-tetrabromopyrrole.
Next, Bmp8 (D), a unique thioredoxin-like dehalogenase, removes the C-2 bromine of tetrabromopyrrole, which then allows for coupling to the previously described 2,4-dibromophenol via the cytochrome P450 enzyme, Bmp7 (C).
The biosynthesis of pentabromopseudilin, among other halopyrroles, has been elucidated via the identification of the conserved brominated marine pyrroles/phenols (bmp) pathway first identified in the marine bacteria, P. luteoviolacea 2ta16 and P. phenolica O-BC30. The bmp pathway describes a bi-modular scheme for polybrominated marine microbial natural products production. In the first module, the bromophenol moiety of PBP is first assembled from a chorismate precursor which is then converted by Bmp6, a chorismate lyase (CL), to yield 4-HBA. 4-HBA is then di-halogenated by the flavin-dependent halogenase, Bmp5 (Hal), to yield 2,3-dibromophenol.
Consistent with earlier isotopic studies, the PBP halopyrrole biosynthesis via the bmp pathway begins with L-proline. In this module, L-proline is acylated to the acyl carrier protein domain of Bmp1 (ACP-thioesterase (TE) di-domain protein) by the proline adenyl transferase Bmp4 (A).  The flavin-dependent dehydrogenase, Bmp3 (DH), then oxidizes the prolyl ring to a pyrrole. The loaded protein is then tri-brominated with the flavin-dependent halogenase, Bmp2 (Hal), becoming 2,3,4,5-tetrabromopyrrole. Next, Bmp8 (D), a unique thioredoxin-like dehalogenase, removes the C-2 bromine of tetrabromopyrrole, which then allows for coupling to the previously described 2,4-dibromophenol via the cytochrome P450 enzyme, Bmp7 (C).
Pentabromopseudilin