Expasy logo

ENZYME

ENZYME entry: EC 1.14.19.57

Accepted Name
1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] brominase
Reaction catalysed
(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + 3 bromide + 3 FADH2 + 3 O2 <=> (3,4,5-tribromo-1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + 3 FAD + 6 H2O
Comment(s)
  • 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 1.14.19.56, 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.
Cross-references
BRENDA1.14.19.57
EC2PDB1.14.19.57
ExplorEnz1.14.19.57
PRIAM enzyme-specific profiles1.14.19.57
KEGG Ligand Database for Enzyme Nomenclature1.14.19.57
IUBMB Enzyme Nomenclature1.14.19.57
IntEnz1.14.19.57
MEDLINEFind literature relating to 1.14.19.57
MetaCyc1.14.19.57
Rhea expert-curated reactions1.14.19.57
UniProtKB/Swiss-Prot
V4HJ70, BMP2_PSEL2

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot 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.-.-.-