2oa1 | pdb_00002oa1
From Proteopedia
Crystal Structure of RebH, a FAD-dependent halogenase from Lechevalieria aerocolonigenes, the L-Tryptophan with FAD complex
| ||||||||||||
Structural highlights
Function[REBH_NOCAE] Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyze the chlorination of tryptophan (Trp) at C7 position to yield 7-chlorotryptophan. The reaction between FADH2, Cl-, and O2 generates the powerful oxidant HOCl, which is presumed to carry out the chlorination reaction. The reaction of HOCl with the active site Lys-79 generates a lysine chloramine, which plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes. It is also able to use bromide ions to generate monobrominated Trp.[1] [2] [3] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
| ||||||||||||||||||||||
This page was last modified 12:50, 9 June 2021.