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:*'''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 | ||
| - | There are <scene name='75/752267/Sheets_vs_helix/2'>10 alpha helices and 8 beta sheets</scene> | + | There are <scene name='75/752267/Sheets_vs_helix/2'>10 alpha helices and 8 beta sheets</scene>. The structure of the YfeX monomer shows traits related to the Dyp super family in that the beta strands are anti- parallel. The N and C terminal domains are connected by a twenty amino acid long loop. |
Revision as of 01:58, 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.
