TY  - CHAP
AU  - Veljović-Jovanović, Sonja
AU  - Kukavica, Biljana
AU  - Vidović, Marija
AU  - Morina, Filis
AU  - Menckhoff, Ljiljana
PY  - 2018
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1185
AB  - Class III peroxidases (POXs; EC. 1.11.1.7), are secretory, multifunctional plant enzymes that catalyze the oxidation of a variety of substrates by hydrogen peroxide (H2O2). They show a remarkable diversity of isoenzymes, are encoded by a large number of paralogous genes, and are involved in a broad range of metabolic processes throughout plant growth and development. Peroxidases isoenzymes are located in the cell wall, apoplast and vacuole, and may be either soluble or ionically and covalently cell wall bound. They are involved in cell wall cross-linking and loosening, lignification and suberization, auxin catabolism and secondary metabolism. Due to their ability to control the levels of reactive oxygen species (ROS), POXs are efficient components of the antioxidative system induced in response to environmental stress, such as pathogen attack, metal excess, salinity, drought and high light intensity. In addition to the peroxidative function, POXs can catalyze H2O2 production in the oxidative cycle. Peroxidases are responsible either for cell elongation or cell wall stiffening, affecting carbon allocation, auxin level and redox homeostasis, which implicates their key role as being in the regulation of growth and defence under stress condition. This chapter will discuss novel insights into the functions of PODs with special emphasis on their localization, substrate specificity and the regulation of redox homeostasis.
PB  - Springer International Publishing
T2  - Antioxidants and Antioxidant Enzymes in Higher Plants
T1  - Class III peroxidases: Functions, localization and redox regulation of isoenzymes
EP  - 300
SP  - 269
DO  - 10.1007/978-3-319-75088-0_13
ER  - 

@inbook{
author = "Veljović-Jovanović, Sonja and Kukavica, Biljana and Vidović, Marija and Morina, Filis and Menckhoff, Ljiljana",
year = "2018",
abstract = "Class III peroxidases (POXs; EC. 1.11.1.7), are secretory, multifunctional plant enzymes that catalyze the oxidation of a variety of substrates by hydrogen peroxide (H2O2). They show a remarkable diversity of isoenzymes, are encoded by a large number of paralogous genes, and are involved in a broad range of metabolic processes throughout plant growth and development. Peroxidases isoenzymes are located in the cell wall, apoplast and vacuole, and may be either soluble or ionically and covalently cell wall bound. They are involved in cell wall cross-linking and loosening, lignification and suberization, auxin catabolism and secondary metabolism. Due to their ability to control the levels of reactive oxygen species (ROS), POXs are efficient components of the antioxidative system induced in response to environmental stress, such as pathogen attack, metal excess, salinity, drought and high light intensity. In addition to the peroxidative function, POXs can catalyze H2O2 production in the oxidative cycle. Peroxidases are responsible either for cell elongation or cell wall stiffening, affecting carbon allocation, auxin level and redox homeostasis, which implicates their key role as being in the regulation of growth and defence under stress condition. This chapter will discuss novel insights into the functions of PODs with special emphasis on their localization, substrate specificity and the regulation of redox homeostasis.",
publisher = "Springer International Publishing",
journal = "Antioxidants and Antioxidant Enzymes in Higher Plants",
booktitle = "Class III peroxidases: Functions, localization and redox regulation of isoenzymes",
pages = "300-269",
doi = "10.1007/978-3-319-75088-0_13"
}

Veljović-Jovanović, S., Kukavica, B., Vidović, M., Morina, F.,& Menckhoff, L.. (2018). Class III peroxidases: Functions, localization and redox regulation of isoenzymes. in Antioxidants and Antioxidant Enzymes in Higher Plants
Springer International Publishing., 269-300.
https://doi.org/10.1007/978-3-319-75088-0_13

Veljović-Jovanović S, Kukavica B, Vidović M, Morina F, Menckhoff L. Class III peroxidases: Functions, localization and redox regulation of isoenzymes. in Antioxidants and Antioxidant Enzymes in Higher Plants. 2018;:269-300.
doi:10.1007/978-3-319-75088-0_13 .

Veljović-Jovanović, Sonja, Kukavica, Biljana, Vidović, Marija, Morina, Filis, Menckhoff, Ljiljana, "Class III peroxidases: Functions, localization and redox regulation of isoenzymes" in Antioxidants and Antioxidant Enzymes in Higher Plants (2018):269-300,
https://doi.org/10.1007/978-3-319-75088-0_13 . .

TY  - JOUR
AU  - Kukavica, Biljana
AU  - Veljović-Jovanović, Sonja
AU  - Menckhoff, Ljiljana
AU  - Luethje, Sabine
PY  - 2012
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/579
AB  - Cell wall isolated from pea roots was used to separate and characterize two fractions possessing class III peroxidase activity: (i) ionically bound proteins and (ii) covalently bound proteins. Modified SDS-PAGE separated peroxidase isoforms by their apparent molecular weights: four bands of 56, 46, 44, and 41 kDa were found in the ionically bound fraction (iPOD) and one band (70 kDa) was resolved after treatment of the cell wall with cellulase and pectinase (cPOD). Isoelectric focusing (IEF) patterns for iPODs and cPODs were significantly different: five iPODs with highly cationic pI (9.5-9.2) were detected, whereas the nine cPODs were anionic with pI values between pH 3.7 and 5. iPODs and cPODs showed rather specific substrate affinity and different sensitivity to inhibitors, heat, and deglycosylation treatments. Peroxidase and oxidase activities and their IEF patterns for both fractions were determined in different zones along the root and in roots of different ages. New iPODs with pI 9.34 and 9.5 were induced with root growth, while the activity of cPODs was more related to the formation of the cell wall in non-elongating tissue. Treatment with auxin that inhibits root growth led to suppression of iPOD and induction of cPOD. A similar effect was obtained with the widely used elicitor, chitosan, which also induced cPODs with pI 5.3 and 5.7, which may be specifically related to pathogen defence. The differences reported here between biochemical properties of cPOD and iPOD and their differential induction during development and under specific treatments implicate that they are involved in specific and different physiological processes.
PB  - Oxford Univ Press, Oxford
T2  - Journal of Experimental Botany
T1  - Cell wall-bound cationic and anionic class III isoperoxidases of pea root: biochemical characterization and function in root growth
EP  - 4645
IS  - 12
SP  - 4631
VL  - 63
DO  - 10.1093/jxb/ers139
ER  - 

@article{
author = "Kukavica, Biljana and Veljović-Jovanović, Sonja and Menckhoff, Ljiljana and Luethje, Sabine",
year = "2012",
abstract = "Cell wall isolated from pea roots was used to separate and characterize two fractions possessing class III peroxidase activity: (i) ionically bound proteins and (ii) covalently bound proteins. Modified SDS-PAGE separated peroxidase isoforms by their apparent molecular weights: four bands of 56, 46, 44, and 41 kDa were found in the ionically bound fraction (iPOD) and one band (70 kDa) was resolved after treatment of the cell wall with cellulase and pectinase (cPOD). Isoelectric focusing (IEF) patterns for iPODs and cPODs were significantly different: five iPODs with highly cationic pI (9.5-9.2) were detected, whereas the nine cPODs were anionic with pI values between pH 3.7 and 5. iPODs and cPODs showed rather specific substrate affinity and different sensitivity to inhibitors, heat, and deglycosylation treatments. Peroxidase and oxidase activities and their IEF patterns for both fractions were determined in different zones along the root and in roots of different ages. New iPODs with pI 9.34 and 9.5 were induced with root growth, while the activity of cPODs was more related to the formation of the cell wall in non-elongating tissue. Treatment with auxin that inhibits root growth led to suppression of iPOD and induction of cPOD. A similar effect was obtained with the widely used elicitor, chitosan, which also induced cPODs with pI 5.3 and 5.7, which may be specifically related to pathogen defence. The differences reported here between biochemical properties of cPOD and iPOD and their differential induction during development and under specific treatments implicate that they are involved in specific and different physiological processes.",
publisher = "Oxford Univ Press, Oxford",
journal = "Journal of Experimental Botany",
title = "Cell wall-bound cationic and anionic class III isoperoxidases of pea root: biochemical characterization and function in root growth",
pages = "4645-4631",
number = "12",
volume = "63",
doi = "10.1093/jxb/ers139"
}

Kukavica, B., Veljović-Jovanović, S., Menckhoff, L.,& Luethje, S.. (2012). Cell wall-bound cationic and anionic class III isoperoxidases of pea root: biochemical characterization and function in root growth. in Journal of Experimental Botany
Oxford Univ Press, Oxford., 63(12), 4631-4645.
https://doi.org/10.1093/jxb/ers139

Kukavica B, Veljović-Jovanović S, Menckhoff L, Luethje S. Cell wall-bound cationic and anionic class III isoperoxidases of pea root: biochemical characterization and function in root growth. in Journal of Experimental Botany. 2012;63(12):4631-4645.
doi:10.1093/jxb/ers139 .

Kukavica, Biljana, Veljović-Jovanović, Sonja, Menckhoff, Ljiljana, Luethje, Sabine, "Cell wall-bound cationic and anionic class III isoperoxidases of pea root: biochemical characterization and function in root growth" in Journal of Experimental Botany, 63, no. 12 (2012):4631-4645,
https://doi.org/10.1093/jxb/ers139 . .