Plant Catalases

Heinze, Michael; Gerhardt, Bernt

doi:10.1007/978-94-015-9858-3_4

Cited by 15 publications

(12 citation statements)

References 150 publications

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“…Plants contain monofunctional, tetrameric and heme-containing catalases that are mostly localized in peroxisomes or glyoxysomes [13,20]. In photosynthesizing green leaves, H 2 O 2 is produced mainly in the peroxisomes by the oxidation of glycolate during photorespiration or in the chloroplasts through the univalent reduction of O 2 by phothosystem I in the Mehler reaction and a subsequent dismutation of the superoxide.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of the catalase activity from Phaseolus vulgaris and Medicago sativa by sodium chloride

García

Iribarne

Palma

et al. 2007

Plant Physiology and Biochemistry

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Section: Introductionmentioning

confidence: 99%

Inhibition of the catalase activity from Phaseolus vulgaris and Medicago sativa by sodium chloride

García

Iribarne

Palma

et al. 2007

Plant Physiology and Biochemistry

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“…1981). A database search indicated that catalase polypeptides designated as HNNCATA3 and HNNCATA4, which are enriched in the peroxisomal cores of sunflower leaves (Heinze & Gerhardt 2002), were highly homologous (95.3% identity between HaCAT‐1 and HNNCATA3) to HaCAT‐1 of H. alpina . Interestingly, Eising et al .…”

Section: Resultsmentioning

confidence: 99%

“…We did not observe the higher apparent molecular mass of 59 kDa that was reported previously(Tenberge et al . 1997; Heinze & Gerhardt 2002).…”

Section: Resultsmentioning

confidence: 99%

“…The most marked difference was the low specific activity of HaCAT‐1 (Table 1). Similarly, the specific activity of the core isozymes of sunflower catalases accounted for only 10% of that of the light‐sensitive matrix isozymes (Eising & Gerhardt 1986; Heinze & Gerhardt 2002).…”

Section: Discussionmentioning

confidence: 99%

“…Plants contain monofunctional, tetrameric and heme‐containing catalases that are mostly localized in peroxisomes or glyoxysomes (Willekens et al . 1995; Heinze & Gerhardt 2002; Feierabend 2005). In photosynthesizing green leaves, H 2 O 2 is produced mainly in the peroxisomes by the oxidation of glycolate during photorespiration or in the chloroplasts through the univalent reduction of O 2 by photosystem I in the Mehler reaction and a subsequent dismutation of the superoxide.…”

Section: Introductionmentioning

confidence: 99%

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Molecular identification, heterologous expression and properties of light‐insensitive plant catalases

Engel

Schmidt

Feierabend

2005

Plant Cell & Environment

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Most catalases are inactivated by light in a heme-sensitized and O 2 -dependent reaction. In leaves of the alpine plant Homogyne alpina and in the peroxisomal cores of Helianthus annuus , light-insensitive catalases were observed. For the catalases Hacat1 of H. alpina and HnncatA3 of H. annuus , cDNA clones were obtained. Expression of recombinant active enzymes in insect cells confirmed that they coded for light-insensitive catalases. Kinetic and catalytic properties of light-sensitive or light-insensitive catalases did not differ substantially. However, the specific activity of the latter was markedly lower. The light-insensitive catalase HaCAT-1 was not resistant against inactivation by superoxide. Amino acid sequences of the light-insensitive catalases HaCAT-1 and HNNCATA3 were highly identical. They showed only a few exceptional amino acid substitutions at positions that are highly conserved in other catalases. These appeared to be localized mainly in a surface cavity at the entrance of a minor channel leading to the central heme, suggesting that this region played some, though yet undefined, role for light sensitivity. While the replacement of a highly conserved His by Thr225 was the most unique substitution, a single exchange of His225 by Thr in the light-sensitive catalase SaCAT-1 by mutagenesis was not sufficient to reduce its sensitivity to photoinactivation.

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Plant Peroxisomes and Glyoxysomes

Donaldson

Kwak

Yanik

et al. 2008

Encyclopedia of Life Sciences

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Peroxisomes and glyoxysomes are membrane enclosures containing enzymes that participate in photorespiration in leaves, nitrogen metabolism in root nodules and fat conversions in seeds. Oxidases in these organelles circumvent energy conservation by producing hydrogen peroxide, which is detoxified by catalase in the matrix and ascorbate peroxidase in the membrane. Some hydrogen peroxide may oxidize proteins within the organelles or function as a signalling molecule. Processes in these organelles also produce hormones (jasmonic acid, indole acetic acid). Peroxisomal proteins are brought in from the cytosol by peroxisomal targeting sequences (PTS). The recognition of the PTS and translocation into the organelles are processes conducted by Peroxins. Genomic and proteomic analyses have recently revealed that plant peroxisomes and glyoxysomes can contain over a 100 different protein molecules, many having unknown functions.

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Plant Catalases

Cited by 15 publications

References 150 publications

Inhibition of the catalase activity from Phaseolus vulgaris and Medicago sativa by sodium chloride

Inhibition of the catalase activity from Phaseolus vulgaris and Medicago sativa by sodium chloride

Molecular identification, heterologous expression and properties of light‐insensitive plant catalases

Plant Peroxisomes and Glyoxysomes

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