4x8e

Publication Abstract from PubMed

The non-heme iron enzyme EgtB catalyzes O2 -dependent CS bond formation between gamma-glutamyl cysteine and N-alpha-trimethyl histidine as the central step in ergothioneine biosynthesis. Both, the catalytic activity and the architecture of EgtB are distinct from known sulfur transferases or thiol dioxygenases. The crystal structure of EgtB from Mycobacterium thermoresistibile in complex with gamma-glutamyl cysteine and N-alpha-trimethyl histidine reveals that the two substrates and three histidine residues serve as ligands in an octahedral iron binding site. This active site geometry is consistent with a catalytic mechanism in which CS bond formation is initiated by an iron(III)-complexed thiyl radical attacking the imidazole ring of N-alpha-trimethyl histidine.

Structure of the Sulfoxide Synthase EgtB from the Ergothioneine Biosynthetic Pathway.,Goncharenko KV, Vit A, Blankenfeldt W, Seebeck FP Angew Chem Int Ed Engl. 2015 Jan 16. doi: 10.1002/anie.201410045. PMID:25597398^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.