Sandbox ggc5
From Proteopedia
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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 <ref>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.</ref>. When loaded with heme, the YfeX becomes an effective Dyp and can decolorize alazine red and degrade anthraquinone dye. | 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 <ref>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.</ref>. When loaded with heme, the YfeX becomes an effective Dyp and can decolorize alazine red and degrade anthraquinone dye. | ||
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== Disease == | == 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. | |
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== Structural highlights == | == Structural highlights == | ||
Revision as of 00:59, 1 May 2017
Dye-decolorizing Peroxidase YfeX from Escherichia Coli
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ 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.
