ENZYME entry: EC 18.104.22.168
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|1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] brominase.
|1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FADH(2) + 3 bromide + 3 O(2) <=> 3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FAD + 6 H(2)O|
- The enzyme, characterized from marine bacteria of the
Pseudoalteromonas genus, belongs to a family of FAD-dependent
halogenases that act on acyl-carrier protein-tethered substrates.
- It catalyzes three successive rounds of bromination.
- While the order has not been verified, it is believed to resemble
that of EC 22.214.171.124, due to significant sequence homology.
- Reduced FAD is provided in situ by a dedicated reductase and diffuses
into the active site, where it reacts with the oxygen and bromide
ion, resulting in formation of a bromoamine intermediate on a
catalytic lysine side chain, and the eventual transfer of the bromide
to the substrate.
- The enzyme from Pseudoalteromonas luteoviolacea 2ta16 is specific for
bromide and does not accept chloride.
|PRIAM enzyme-specific profiles||126.96.36.199|
|KEGG Ligand Database for Enzyme Nomenclature||188.8.131.52|
|IUBMB Enzyme Nomenclature||184.108.40.206|
|MEDLINE||Find literature relating to 220.127.116.11|
entries corresponding to 1.14.19.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-