Function
YfeX is a dye-decolorizing peroxidase that has a very high specificity for its substrate. This protein belongs to the heme super family known as Dyp and has recently been discovered in bacteria and fungi [1]. When loaded with heme, the YfeX becomes an effective Dyp and can decolorize alazine red and degrade anthraquinone dye [2]
Disease
The dye-decolorizing peroxidase YfeX is present in E. Coli bacteria and has been thought to be used as a method to obtain the iron necessary for survival from the heme group of its hosts. Research has been done to find the correlation between the two. Although no hard evidence has been obtained, there is still reason to believe there is a connection between the peroxidase and the means for iron acquisition.
Structural highlights
The YfeX Dyp contains four . These heme groups are surrounded by that are conserved across this peroxidase super family. (His 215-purple, Asp 143-blue, Arg 232-yellow)
- His 215: proximal axial ligand of the heme iron atom
- Asp 143 and Arg 232: Catalytic role varies with divergence of substrate and substrate type
There are . The structure of the YfeX monomer shows traits related to the Dyp super family in that the β-strands are anti- parallel. The N and C terminal domains are connected by a twenty amino acid long loop.
