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Bacterial Scavengase p20 Is Structurally and Functionally Related to Peroxiredoxins
Journal article   Open access   Peer reviewed

Bacterial Scavengase p20 Is Structurally and Functionally Related to Peroxiredoxins

Yuan Zhou, Xiao-Yu Wan, Hai-Lin Wang, Zi-Ying Yan, Yun De Hou and Dong-Yan Jin
Biochemical and biophysical research communications, Vol.233(3), pp.848-852
04/28/1997
DOI: 10.1006/bbrc.1997.6564
PMID: 9168946
url
https://doi.org/10.1006/bbrc.1997.6564View
Published (Version of record) Open Access

Abstract

Scavengase p20 was recently identified as a novel family of bacterial antioxidant enzymes possessing thioredoxin-linked thiol peroxidase activity. In this study, theEscherichia coligene coding for scavengase p20 was isolated from three different strains and the nucleotide sequence was determined. Multiple alignment of amino acid sequence revealed that a previously unidentified Cys-61 is most conserved among all bacterial p20 scavengases and corresponds to the active site in the well-characterized peroxiredoxins. Phylogenetic analysis further supported that scavengase p20 is a novel subfamily of peroxiredoxins. Site-directed mutagenesis studies demonstrated that Cys-61 is indispensable for the antioxidant activities of scavengase p20. Taken together, our findings strongly suggest that the p20 scavengases are structurally and functionally related to peroxiredoxins.

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