Disease relevance of Pfl_5416

• Anaerobiosis had no effect on the toxicity of either p-benzoquinone or the peroxidase reaction and the generation of superoxide and hydroxyl radicals catalyzed by xanthine oxidase was not bactericidal [1].
• For the three Gram-negative bacteria, Pseudomonas fluorescens, Escherichia coli, and Erwinia amylovora, p-benzoquinone was the principal bactericidal agent formed in vitro during the oxidation of hydroquinone by horseradish peroxidase, whereas no toxicity could be associated with either phenolic or oxygen-free radicals [1].
• Smc01944, a secreted peroxidase induced by oxidative stresses in Sinorhizobium meliloti 1021 [2].
• It appears that the Lactobacillus strains synthetize one or more inhibitive substances instable in cold or heat, sensitive to the enzyme activity of peroxidase and to certain proteolytic enzymes (protease isolated from Bacillus subtilis and pepsin) [3].

High impact information on Pfl_5416

• Even the continuous generation of p-benzosemiquinone during the simultaneous reduction of p-benzoquinone by xanthine oxidase and reoxidation of hydroquinone by peroxidase was no more toxic than p-benzoquinone alone [1].
• Peroxidase-labeled concanavalin A (ConA) and wheat germ agglutinin (WGA) were used, as they specifically bind to saccharide residues most frequently encountered in biofilms matrices: D-glucose or D-mannose for ConA and N-acetyl-D-glucosamine or N-acetylneuraminic acid for WGA [4].
• A peroxidase and another enzymatic activity referred to as a polyphenol oxidase were found to be involved in the oxidation of 4-chlorocatechol to 4-chloro-1,2-benzoquinone, i.e. in the production of highly reactive substrates for pigment formation [5].
• Polymerization of cardanol using soybean peroxidase and its potential application as anti-biofilm coating material [6].
• Soybean peroxidase (20 mg) catalyzed the oxidative polymerization of cardanol in 2-propanol/phospate buffer solution (25 ml, 1:1 v/v) and yielded 62% polycardanol over 6 h [6].

Chemical compound and disease context of Pfl_5416

• The optimal components in the reagents are: cholesterol oxidase 250 (Nocardia erythropolis), 250 (Streptomyces sp), or 300 (Pseudomonas fluorescens) U/L, cholesterol esterase 200 U/L, peroxidase 10,000 U/L, sodium cholate 3 mmol/L, 4-aminoantipyrine 0.5 mmol/L, phenol 20 mmol/L, Triton X-100 2 mL/L, and phosphate buffer, pH 7 [7].

Associations of Pfl_5416 with chemical compounds

• In P. fluorescens-treated plants, the peroxidase and phenylalanine ammonia-lyase activity increased [8].

References