A Retrospective Look at the Cationic Peanut Peroxidase Structure

Abstract

The cationic peanut peroxidase has been studied in detail, not only with regard to its peptide structure, but also to the sites and role of the three moieties linked to it. Peanut peroxidase lends itself well to a close examination as a potential example for other plant peroxidase studies. It was the first plant peroxidase for which a 3-D structure was derived from crystals, with the glycans intact. Subsequent analysis of peroxidases structures from other plants have not shown great differences to that of the peanut peroxidase. As the period of proteomics follows on the era of genomics, the study of glycans has been brought back into focus. With the potential use of peroxidase as a polymerization agent for industry, there are some aspects of the overall structure that should be kept in mind for successful use of this enzyme. A variety of techniques are now available to assay for these structures/moieties and their roles. Peanut peroxidase data are reviewed in that light, as well as defining some true terms for isozymes. Because a high return of the enzyme in a pure form has been obtained from cultured cells in suspension culture, a brief review of this is also offered.

Purification and partial characterization of a thermostable peroxidase isoenzyme from Vigna sp seedlings

“…The calculated molecular weight (40.3 KD) is also in the range of the given molecular weights for other classical plant peroxidases. Indeed, this molecular weight is similar to that of horseradish (44 kD) (Welinder, 1979), tobacco (37 kD) (Gazaryan and Lagrimini, 1996), sweet potato (37 kD) (Leon et al, 2002), peanut (37-40 kD) (Van Huystee et al, 2003) and soybean peroxidases (37 kD) (Gilliken and Graham, 1991).…”

Purification and characterisation of two acidic peroxidase isoforms from the sheaths of bamboo shoots

“…This value was much higher than the reported peroxidases from other sources, such as palm tree (51 and 57 kDa) (Sakharov, 2004), horseradish (44 kDa) (Welinder, 1979), bitter gourd (43 kDa) (Fatima & Husain, 2007), tobacco (37 kDa) (Gazaryan & Lagrimini, 1996), sweet potato (37 kDa) (Castillo Leon et al. , 2002), peanut (37–40 kDa) (Van Huystee et al. , 2002), and soybean peroxidase (37 kDa) (Gillikin & Graham, 1991).…”

Post‐translational modification and extended glycosylation pattern of a plant latex peroxidase of native source characterized by X‐ray crystallography

“…Similarly, other plant peroxidases from horseradish, Japanese radish, turnip and oil palm leaf have also been reported to contain approximately 18%, 12–18%, 20% and 37% carbohydrate, respectively . The precise function of glycans for peroxidases is not clearly demonstrated, except for cationic peanut peroxidase where the glycans may play a role in secretion . In general, the glycans are involved in protecting proteins from degradation, increased solubility and transport inside the cell .…”

“…In general, the glycans are involved in protecting proteins from degradation, increased solubility and transport inside the cell . The nonglycosylated peroxidase loses its secretory function and leads to the degradation of the protein within the cell .…”