Mitochondrial glycolate oxidation contributes to photorespiration in higher plants
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چکیده
منابع مشابه
Mitochondrial glycolate oxidation contributes to photorespiration in higher plants.
The oxidation of glycolate to glyoxylate is an important reaction step in photorespiration. Land plants and charophycean green algae oxidize glycolate in the peroxisome using oxygen as a co-factor, whereas chlorophycean green algae use a mitochondrial glycolate dehydrogenase (GDH) with organic co-factors. Previous analyses revealed the existence of a GDH in the mitochondria of Arabidopsis thali...
متن کاملTwo alanine aminotranferases link mitochondrial glycolate oxidation to the major photorespiratory pathway in Arabidopsis and rice
The major photorespiratory pathway in higher plants is distributed over chloroplasts, mitochondria, and peroxisomes. In this pathway, glycolate oxidation takes place in peroxisomes. It was previously suggested that a mitochondrial glycolate dehydrogenase (GlcDH) that was conserved from green algae lacking leaf-type peroxisomes contributes to photorespiration in Arabidopsis thaliana. Here, the i...
متن کاملAlternate pathways of glycolate synthesis in tobacco and maize leaves in relation to rates of photorespiration.
After a preliminary period in light, leaf disks floated on 10 mm alpha-hydroxy-2-pyridinemethanesulfonic acid to inhibit glycolate oxidase accumulate glycolate at average initial rates of 67 micromoles in tobacco and 8 micromoles per gram fresh weight per hour in maize under optimal conditions in air. In the presence of (14)CO(2), the glycolate synthesized has a high specific radioactivity in i...
متن کاملThe recognition of glycolate oxidase apoprotein with flavin analogs in higher plants.
The dependence of glycolate oxidase apoprotein (apoGO) activity on flavin analogs was surveyed in 9 higher plants from 7 families. Activities of all apoGOs depended not only on flavin mononucleotide (FMN) but also on flavin adenine dinucleotide (FAD), but not on riboflavin. The kinetic analysis showed that FMN was the optimum cofactor for apoGO from leaves of Brassica campestris. In plant kingd...
متن کاملIdentification, separation, and characterization of acyl-coenzyme A dehydrogenases involved in mitochondrial beta-oxidation in higher plants
The existence in higher plants of an additional beta-oxidation system in mitochondria, besides the well-characterized peroxisomal system, is often considered controversial. Unequivocal demonstration of beta-oxidation activity in mitochondria should rely on identification of the enzymes specific to mitochondrial beta-oxidation. Acyl-coenzyme A dehydrogenase (ACAD) (EC 1.3.99.2,3) activity was de...
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ژورنال
عنوان ژورنال: Journal of Experimental Botany
سال: 2007
ISSN: 0022-0957,1460-2431
DOI: 10.1093/jxb/erm131