The Enzyme Database

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Accepted name: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] brominase
Reaction: 1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FADH2 + 3 bromide + 3 O2 = 3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + 3 FAD + 6 H2O (overall reaction)
(1a) 1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2 = 5-bromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
(1b) 5-bromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2 = 4,5-dibromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
(1c) 4,5-dibromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FADH2 + bromide + O2 = 3,4,5-tribromo-1H-pyrrole-2-carbonyl-[Bmp1 peptidyl-carrier protein] + FAD + 2 H2O
Other name(s): bmp2 (gene name)
Systematic name: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein]:FADH2 oxidoreductase (brominating)
Comments: 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 catalyses three successive rounds of bromination. While the order has not been verified, it is believed to resemble that of EC, S-(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] chlorinase, 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Agarwal, V., El Gamal, A.A., Yamanaka, K., Poth, D., Kersten, R.D., Schorn, M., Allen, E.E. and Moore, B.S. Biosynthesis of polybrominated aromatic organic compounds by marine bacteria. Nat. Chem. Biol. 10 (2014) 640–647. [DOI] [PMID: 24974229]
[EC created 2018]

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