Sandbox ggc5
From Proteopedia
(Difference between revisions)
| (3 intermediate revisions not shown.) | |||
| Line 16: | Line 16: | ||
The YfeX Dyp contains four <scene name='75/752267/Heme_groups/1'>Heme groups</scene>. These heme groups are surrounded by <scene name='75/752267/Amino_acids/1'>three amino acid residues</scene> that are conserved across this peroxidase super family. (His 215-purple, Asp 143-blue, Arg 232-yellow) | The YfeX Dyp contains four <scene name='75/752267/Heme_groups/1'>Heme groups</scene>. These heme groups are surrounded by <scene name='75/752267/Amino_acids/1'>three amino acid residues</scene> 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 <scene name='75/752267/Sheets_vs_helix/ | + | There are <scene name='75/752267/Sheets_vs_helix/4'>10 α-helices and 8 β-sheets</scene>. 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. |
Current revision
Dye-decolorizing Peroxidase YfeX from Escherichia Coli
| |||||||||||
References
- ↑ Xiuhua Liu, Z. Y. (2017). Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp143 and Arg232 play divergent roles toward different substrates. Biochemical and Biophysical Research Communications, 40-44.
- ↑ Xiuhua Liu, Z. Y. (2017). Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp143 and Arg232 play divergent roles toward different substrates. Biochemical and Biophysical Research Communications, 40-44.
