Sandbox ggc5
From Proteopedia
(Difference between revisions)
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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 | **'''Asp 143 and Arg 232''': Catalytic role varies with divergence of substrate and substrate type | ||
Revision as of 01:49, 1 May 2017
Dye-decolorizing Peroxidase YfeX from Escherichia Coli
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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.
