The Effects of the Site-Directed Removal of N-Glycosylation from Cationic Peanut Peroxidase on Its Function

Lige, Bao; Ma, Shengwu; Huystee, Robert B. van

doi:10.1006/abbi.2000.2187

Cited by 70 publications

(63 citation statements)

References 38 publications

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“…The amino acid sequences were found to be highly variable within the plant peroxidase superfamily, with less than 20% identity in the most divergent cases. The majority of these enzymes are N-glycosylated and are predicted to be localized in cell walls or in vacuoles (Lige et al 2001).…”

Section: Class III Plant Peroxidasesmentioning

confidence: 99%

Plant peroxidases: biomarkers of metallic stress

Jouili¹,

Bouazizi²,

Ferjani³

2011

Acta Physiol Plant

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The term ''peroxidase'' designs a group of hemoproteins with a wide structural variability. These enzymes catalyze the redox reaction between hydrogen peroxide and some reductors. They can be found in animals, plants and microorganisms. In plants, peroxidases are involved in numerous cellular processes such as development and stress responses. In fact, they are involved in growth regulation by controlling hormonal and cell wall metabolism and antioxidant defense. On the other hand, these enzymes are considered as a biomarker indicating biotic and abiotic stresses. Under metallic stress conditions, the quantitative and qualitative profiles of peroxidases are generally modified. Such modulations could prove the major role played by these enzymes in the defense mechanism. In this paper, we discussed the variation of isoperoxidases behavior under metallic stress conditions.

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Section: Class III Plant Peroxidasesmentioning

confidence: 99%

Plant peroxidases: biomarkers of metallic stress

Jouili¹,

Bouazizi²,

Ferjani³

2011

Acta Physiol Plant

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“…Differences in the glycosylation patterns and surface charges among the peroxidase protein family members could also potentially be involved in the determination of substrate specificity. In the case of the cationic peanut peroxidase, site-directed removal of each of the three N-linked complex glycans revealed that the N-60 and N-144 glycans influence the peroxidase catalytic activity, whereas the N-185 glycan is important for the thermostability of the enzyme (Lige et al, 2001). It has been postulated that glycans could affect substrate access because of their large size (Douroupi et al, 2005;Gabaldon et al, 2007), and could affect reaction dynamics due to a dampening of backbone motion (Nielsen et al, 2001).…”

Section: Relationship Between Structure and Function In Class III Permentioning

confidence: 99%

Specific functions of individual class III peroxidase genes

Cosio

Dunand

2009

Journal of Experimental Botany

364

303

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In higher plants, class III peroxidases exist as large multigene families (e.g. 73 genes in Arabidopsis thaliana). The diversity of processes catalysed by peroxidases as well as the large number of their genes suggests the possibility of a functional specialization of each isoform. In addition, the fact that peroxidase promoter sequences are very divergent and that protein sequences contain both highly conserved domains and variable regions supports this hypothesis. However, two difficulties are associated with the study of the function of specific peroxidase genes: (i) the modification of the expression of a single peroxidase gene often results in no visible mutant phenotype, because it is compensated by redundant genes; and (ii) peroxidases show low substrate specificity in vitro resulting in an unreliable indication of peroxidase specific activity unless complementary data are available. The generalization of molecular biology approaches such as whole transcriptome analysis and recombinant DNA combined with biochemical approaches provide unprecedented tools for overcoming these difficulties. This review highlights progress made with these new techniques for identifying the specific function of individual class III peroxidase genes taking as an example the model plant A. thaliana, as well as discussing some other plants.

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“…Glycosylation plays critical role in structure, function, and resulting immune response of several proteins (10)(11)(12)(13)(14)(15)(16). It has been reported that carbohydrates in glycoproteins are important for protein folding (12,13,17), stability (11,18), macromolecular interactions, and activity (19)(20)(21).…”

Section: Introductionmentioning

confidence: 99%

Role of Glycosylation in Conformational Stability, Activity, Macromolecular Interaction and Immunogenicity of Recombinant Human Factor VIII

Kosloski

Miclea

Balu‐Iyer

2009

AAPS J

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Abstract. Factor VIII (FVIII) is a multi-domain glycoprotein that is an essential cofactor in the blood coagulation cascade. Its deficiency or dysfunction causes hemophilia A, a bleeding disorder. Replacement using exogenous recombinant human factor VIII (rFVIII) is the first line of therapy for hemophilia A. The role of glycosylation on the activity, stability, protein-lipid interaction, and immunogenicity of FVIII is not known. In order to investigate the role of glycosylation, a deglycosylated form of FVIII was generated by enzymatic cleavage of carbohydrate chains. The biochemical properties of fully glycosylated and completely deglycosylated forms of rFVIII (degly rFVIII) were compared using enzyme-linked immunosorbent assay, size exclusion chromatography, and clotting activity studies. The biological activity of degly FVIII decreased in comparison to the fully glycosylated protein. The ability of degly rFVIII to interact with phosphatidylserine containing membranes was partly impaired. Data suggested that glycosylation significantly influences the stability and the biologically relevant macromolecular interactions of FVIII. The effect of glycosylation on immunogenicity was investigated in a murine model of hemophilia A. Studies showed that deletion of glycosylation did not increase immunogenicity.

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The Effects of the Site-Directed Removal of N-Glycosylation from Cationic Peanut Peroxidase on Its Function

Cited by 70 publications

References 38 publications

Plant peroxidases: biomarkers of metallic stress

Plant peroxidases: biomarkers of metallic stress

Specific functions of individual class III peroxidase genes

Role of Glycosylation in Conformational Stability, Activity, Macromolecular Interaction and Immunogenicity of Recombinant Human Factor VIII

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