Substrate specificity of plant peroxidases

Chmielnicka, Jadwiga; Ohlsson, Per‐Ingvar; Paul, K. G.; Stigbrand, Torgny

doi:10.1016/0014-5793(71)80143-6

Cited by 20 publications

(5 citation statements)

References 5 publications

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“…The distribution of isoperoxidases between the protoplast and wall bound fractions in the tobacco pith and in potato roots support the repeatedly claimed possibility of differences in the function of particular isoperoxidases or isoperoxidase groups in the cell; the question is raised whether one has to deal with different isoenzymes or different enzymes (9). The reported function of peroxidase as lignin polymerase (21) Contrary to what was expected, the greatest portion (80% and more) of the cell peroxidase was bound to the walls of the very young elongating pith cells.…”

Section: Discussionmentioning

confidence: 58%

Cell Wall and Protoplast Isoperoxidases in Relation to Injury, Indoleacetic Acid, and Ethylene Effects

Birecka¹,

Miller²

1974

Plant Physiol.

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In tobacco (Nicotiana Tabacum) pith, sweet potato (Ipomnoea batatas), and carrot (Daucus carota) storage roots, differences were found between cell wall and protoplast peroxidases in their isoenzyme patterns, activity, and reaction to tissue injury.In the pith of elongating tobacco internodes, 90% of total activity was associated with the walls, 80% of which was due to the ionically and covalently bound fractions. With senescence, the increase in activity occurred mainly in the protoplast and the free fraction in the walls. The major protoplast isoperoxidases formed the free wail fraction, and the minor ones formed the wail bound fractions. The minor isoperoxidases were the only ones whose activities were affected by cut injury. Neither senescence nor injury caused qualitative changes in the cell isoperoxidase pattern. In the potato root cells, the isoperoxidases were also distinctive in their distribution and in their reactions to injury as well as to ethylene.In potato and carrot roots, the wall fractions contributed 30 and 95 %, respectively, to total peroxidase activity. The injury-induced increase in peroxidase activity occurred mainly in the protoplast of tobacco pith and potato roots and almost entirely in the ionically bound fraction of the walls in carrot roots. Ethylene stimulated peroxidase development in potato roots, especially in the protoplast, but had no effect in either tobacco pith or carrot roots. Ethylene did not affect the inhibiting action of indoleacetic acid on peroxidase activity in tobacco pith, nor did indoleacetic acid significantly affect the stimulating action of ethylene in potato roots.Actinomycin D inhibited the injury-dependent development of peroxidase in tobacco pith, stimulated the injury-and ethylene-dependent peroxidase development in potato root, and had no effect on peroxidase development in carrot root. Cycloheximide prevented the increase in peroxidase activity in tobacco pith and potato root, but not in the carrot root. Thus, the enhancement of peroxidase activity resulted from either enzyme activation exclusively or front enzyme synthesis. RNA synthesis seems to be only indirectly related to isoperoxidase synthesis caused bv injury or ethylene.Previous investigation (5) (3,11,25,31) and its possible involvement in cell wall lignification and extensibility has been discussed in detail (10,20,32,35). Therefore, we extended our comparative studies to include the cell wall isoperoxidase fractions. This report deals with the interaction between injury and IAA, cycloheximide, or actinomycin D in the development of the soluble and cell wall bound isoperoxidases in the presence or absence of added ethylene or in the presence of mercuric perchlorate used to remove endogenous ethylene. The reported lack of reaction of carrot root-soluble peroxidase to added ethylene, in contrast to sweet potato root (36), prompted us to include the carrot root in this study. Special attention has been paid to the free peroxidase fraction in tobacco pith cell walls, since a significant r...

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Section: Discussionmentioning

confidence: 58%

Cell Wall and Protoplast Isoperoxidases in Relation to Injury, Indoleacetic Acid, and Ethylene Effects

Birecka¹,

Miller²

1974

Plant Physiol.

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“…3), is most probably the real "specialty of the house" for heme b binding proteins [42,43]. A wide set of oxidases [44], peroxidases [45], peroxygenases [46,47], dioxygenases [48], and monooxygenases [49,50] promote a myriad of reactions, either with high chemo-, regio-, and stereospecificity, or in a promiscuous and unselective manner [51][52][53]. Dioxygen, or its two protons two electron reduced form, hydrogen peroxide, gives rise to a series of highly reactive oxygen species, upon binding to iron(II)-or to iron(III)-heme b species, respectively [54,55].…”

Section: Highlightsmentioning

confidence: 99%

Mimochrome, a metalloporphyrin‐based catalytic Swiss knife†

Leone

Chino

Nastri

et al. 2020

Biotech and App Biochem

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Over the years, mimochromes, a class of miniaturized porphyrin‐based metalloproteins, have proven to be reliable but still versatile scaffolds. After two decades from their birth, we retrospectively review our work in mimochrome design and engineering, which allowed us developing functional models. They act as electron‐transfer miniproteins or more elaborate artificial metalloenzymes, endowed with peroxidase, peroxygenase, and hydrogenase activities. Mimochromes represent simple yet functional synthetic models that respond to metal ion replacement and noncovalent modulation of the environment, similarly to natural heme‐proteins. More recently, we have demonstrated that the most active analogue retains its functionality when immobilized on nanomaterials and surfaces, thus affording bioconjugates, useful in sensing and catalysis. This review also briefly summarizes the most important contributions to heme‐protein design from leading groups in the field.

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“…Peroxidases (EC 1.1 1.1.7) a r e enzymes widely distributed throughout the plant kingdom where they carry out a series of biosynthetic and degradative functions, being apparently involved in phenolic cross-linking and alkaloid metabolism (Chmielnicka er af., 1971;Blom rt af., 1991). O n e of the main problems in assigning a function to peroxidases in oioo lies in the high number of isoforms of the enzyme, each isoenzyme (acidic o r basic) group apparently being involved in different aspects of plant metabolism (Chmielnicka et al, 1971).…”

Section: Introductionmentioning

confidence: 99%

Anomalous behaviour of acidic grapevine peroxidase isoenzymes during preparative isoelectric focusing

Morales

Pedreño

Muñoz

et al. 1994

Phytochemical Analysis

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Preparative isoelectric focusing of grapevine peroxidases on glycerol‐stabilized pH gradients in the RotoforTM cell has been used to purify peroxidase isoenzymes from the spent medium of suspension cultured cells derived from mesocarp tissues of grape (Vitis vinifera cv. Monastrell) berries. The results showed that, under steady‐state conditions, basic peroxidase isoenzymes focus well while acidic peroxidase isoenzymes show anomalous behaviour during isoelectric focusing, leading to diffuse and/or multiband isoelectric focusing patterns. These results suggest that, although preparative isoelectric focusing in glycerol‐stabilized pH gradients using the Rotofor cell may be a powerful tool for isoenzyme purification, the advantages of this technique may be severely hampered by the anomalous behaviour shown by acidic peroxidase isoenzymes during focusing.

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Substrate specificity of plant peroxidases

Cited by 20 publications

References 5 publications

Cell Wall and Protoplast Isoperoxidases in Relation to Injury, Indoleacetic Acid, and Ethylene Effects

Cell Wall and Protoplast Isoperoxidases in Relation to Injury, Indoleacetic Acid, and Ethylene Effects

Mimochrome, a metalloporphyrin‐based catalytic Swiss knife†

Anomalous behaviour of acidic grapevine peroxidase isoenzymes during preparative isoelectric focusing

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