Peanut peroxidase

APX, ascorbate peroxidase PJiP, Arthromyces ramosus peroxidase BPl, barley grain peroxidase CCP, C3dochrome c peroxidase CIP, Coprinus cinereus peroxidase EXAFS, extended X-ray absorption fine structure HRP, horseradish peroxidase HRP Z (where Z = A1-A3, B1-B3, Cl, C2, D, E1-E6, or N), a specific isoenzyme of horseradish peroxidase HS, high-spin lAA, indole-3-acetic acid LIP, hgnin peroxidase LS, low-spin PNP, the major cationic isoenzyme of peanut peroxidase WT, wild-type 5-c, five-coordinate 6-c, six-coordinate. 

Abbreviations APX, ascorbate peroxidase pAPX, pea cytosolic APX CcP, cytochrome c peroxidase HRP, horseradish peroxidase Lip, lignin peroxidase MnP, manganese peroxidase PNP, peanut peroxidase ARP, Arthromyces ramosus peroxidase 5-c/HS, 5-coordinate, high-spin heme 6-c/HS, 6-coordinate, high-spin heme 6-c/LS, 6-coordinate, low-spin heme SHE, standard hydrogen electrode. 

Maranon, M. J. R., Stillman, M. J., and van Huystee, R. B., 1993, CD analysis of co-dependency of calcium and porphyrin for the integrate molecular structure of peanut peroxidase, Biochem. Biophys. Res. Comm. 194 326n333. 

Peanut peroxidase Soybean peroxidase Sweet potato peroxidase... 

PNP, peanut peroxidase TOP, tobacco peroxidase SPP, sweet potato peroxidase recHRP, recombinant wild type (WT) HRP. HRP PhelllTrp, WLP AsnJOVal, HRP AsnJOAsp, are HRP mutants. 

Mason (30) and Pierpoint (31) have described the involvement of o-diphenols in plants and how they contribute to abnormal plant pigmentation. o-Diphenols are oxidized to o-quinones by enzymes of the phenolase complex (o-diphenol O2 oxidoreductase, E.C. 1.10.3.1) and by peroxidase (E.C. 1.11.1.7). o-Quinones react with amino acids, proteins, amines and thiol groups of proteins to polymerize and from reddish-brown pigments. Concentrations of caffeic acid are doubled in both bean (8) and peanut... 

The three-dimensional structures of plant peroxidases from Arabidopsis [112], barley [147], horseradish [112], peanut [111], and soybean [148] have been... 

Peroxidase Horse radish, apple, bean, grape, barley, potato, cucumber, pea, peanut, tomato Ripening of foods, several functions in plants, colour formation (off-) flavour formation. 

Partition properties 970 Peanuts, as source of peroxidase 977 Pechman-Duisberg condensahon 995 Pechmann reachon 680 Pedahaceae 967 Pentachlorophenol 1350... 

Another example on fluorescence lifetimes of beinoproteins peroxidases (donor H2O2, oxidoreductase E.C. 1.11.1.7) are heme enzymes that catalyze oxidative reactions that use hydrogen perox dase as an electron acceptor. The seed coat soybean peroxidase (SBP) belongs to class III of the plant peroxidase super family, which includes horseradish (HRP), barely (BPl) and peanut (PNP) peroxidases. All the en mes of this class contain a protoheme located within a pocket that plays an important role in the catalytic cycle. Soybean peroxidase (SBP) is a glycoprotein of molecular mass equal to 37 kDa. It is a monomer composed of 326 amino acids with a single tryptophan at position 117 (Figure 7.15). 

Chung, S., Maleki, S. J., and Champagne, E.T., Allergenie properties of roasted peanut allergens may be reduced by peroxidase, J. Agric. Food Chem., 52,4541—4545, 2004. 

Newcomb and Stumpf (1952) first described an enzyme system in peanut cotyledons that catalyzed the oxidation of C fatty acids to C i aldehydes with liberation of CO2. In the presence of NAD", the aldehyde is oxidized to the corresponding C i fatty acid which can enter the cycle for further a-oxi-dation (Martin and Stumpf, 1959). The peanut system was described as a peroxidase process for which a H202-generating system was required (Mar-kovetzeta/., 1972). 

Zheng, X., and van Huystee, R. B., 1992, Anionic peroxidase catalysed ascorbic acid and lAA oxidation in the presence of hydrogen peroxide A defence against peroxidative stress in peanut plant. Phytochemistry 31 1895-1898. 

Table 16.28. Thermal inactivation of lipoxygenase and peroxidase in peanuts...

Peroxidases.—Binding of peanut-cell peroxidase by immobilized concanavalin A indicated that the enzyme is a glycoprotein. ... 

---