thevetia/oxidase

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Proteomic analysis and purification of an unusual germin-like protein with proteolytic activity in the latex of Thevetia peruviana.

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CONCLUSIONS The latex from Thevetia peruviana is rich in plant defense proteins, including a 120 kDa cysteine peptidase with structural characteristics similar to germin-like proteins. More than 20,000 plant species produce latex, including Apocynaceae, Sapotaceae, Papaveraceae and Euphorbiaceae. To

Crystal structure and specific location of a germin-like protein with proteolytic activity from Thevetia peruviana

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Peruvianin-I is a cysteine peptidase (EC 3.4.22) purified from Thevetia peruviana. Previous studies have shown that it is the only germin-like protein (GLP) with proteolytic activity described so far. In this work, the X-ray crystal structure of peruvianin-I was determined to a resolution of 2.15 Å

Structural and enzymatic characterization of Peruvianin‑I, the first germin-like protein with proteolytic activity.

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The germin-like protein (GLP) purified from Thevetia peruviana, Peruvianin-I, is the only one described as having proteolytic activity. Therefore, the goal of this study was to investigate the structural features responsible for its enzymatic activity. Although the amino acid sequence of

Botanical-chemical formulations enhanced yield and protection against Bipolaris sorokiniana in wheat by inducing the expression of pathogenesis-related proteins.

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Two experiments (pot and field experiments) were conducted in two consecutive years to evaluate the protective effects of botanical-chemical formulations on physiological, biochemical performance and grain yield of wheat inoculated with Bipolaris sorokiniana. We compared different formulations

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