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Peroxidase From Proso Millet Exhibits Endonuclease-Like Activity

Peroxidase From Proso Millet Exhibits Endonuclease-Like Activity

Xiaodong Cui, Tingfen Wang, Wenming Wang, Hongfei Wang, Zhuanhua Wang

Acta Biochim Biophys Sin (Shanghai). 2019 Jul 10;51(7):688-696.

PMID: 31168624

Abstract:

In this study, the mechanism of DNA cleavage by cationic peroxidase from proso millet (PmPOD) was investigated. PmPOD cleaved supercoiled circular DNA into both nicked circular and linear forms via a cleavage mechanism that resembles those of native endonucleases. Inhibition and ligation studies demonstrated that reactive oxygen species and the ferriprotoporphyrin IX moiety in PmPOD are not involved in PmPOD-mediated DNA cleavage. Similar to other endonucleases, Mg ions considerably enhance the DNA cleavage activity of PmPOD. Further studies suggested that PmPOD can disrupt phosphodiester bonds in DNA and mononucleotides, indicating that it is a phosphatase. The phosphatase activity of PmPOD is higher than that of horseradish peroxidase (HRP), but the peroxidase activity of PmPOD was lower than that of HRP. PmPOD-mediated hydrolytic cleavage of DNA observed in this study is different from those reported for heme proteins. This study provides valuable insights into the distinct mechanisms underlying DNA cleavage by heme proteins.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9003990	Peroxidase from horseradish		9003-99-0	Price

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