• Title/Summary/Keyword: glycolate oxidase

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Effects of Light on Spinach Glycolate Oxidase Gene Expression

  • Park, Yang-Seo;Jin, Yun-Hae;Kim, Young-Chang;Choi, Jung-Do;Cho, Nam-Jeong
    • BMB Reports
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    • v.28 no.3
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    • pp.271-274
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    • 1995
  • Glycolate oxidase is one of the key enzymes in the pathway of photorespiration. In this study we investigated the effects of light on the expression of the spinach glycolate oxidase gene. Continuous exposure to white light resulted in a gradual increase in the steady-state level of glycolate oxidase mRNA within a time period of 2~24 h in both etiolated and dark-adapted green seedlings. A short white light pulse also increased the level of glycolate oxidase mRNA in etiolated seedlings. The mRNA level reached a maximum at 6~8 h after the pulse and decreased by 24 h after the pulse. The induction patterns of the glycolate oxidase gene by white light appeared similar to those of the rbcS gene, indicating that a common or coordinating regulatory system may be involved in the expression of the glycolate oxidase and rbcS genes. A red light pulse induced an increase in the amount of glycolate oxidase mRNA and this effect was reversed by a subsequent far-red light pulse, suggesting that the expression of the glycolate oxidase gene is regulated by phytochrome.

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Activities of Catalase, Glycolate Oxidase, Hydroxypyruvate and NADPH-Glyoxylate Reductases at Different Growing Stages in the Leaves of Rice Plants (벼의 생육시기에 따른 일부 광호흡효소의 활성변화)

  • 권영명
    • Journal of Plant Biology
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    • v.22 no.3
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    • pp.81-84
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    • 1979
  • Catalase, glycolate oxidase, hydroxypyruvate and NADPH-glyoxylate reductases activities in cell free extracts from leaves of 3 cultivars, Suwon 264, IR 36 and Jin Heung of rice plants were studied at different growing stages. Catalase and glycolate oxidase shows inclining activities toward the maximum vegetative growth whereas declining activities in either the enzymes were noticed during the maturing stage. After the photoperiodic condition exhibit increasing hydroxypyruvate and NADPH-glyoxylate reductases activities with time until maturing stage. No significant differences were found in the enzyme activities, and in analytical data of nitrogen, chlorophyll contents, dry weight and soluble proteins among the 3 cultivars.

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Chemical Modification of Residue of Lysine, Tryptophan, and Cysteine in Spinach Glycolate Oxidase

  • Lee, Duk-Gun;Cho, Nam-Jeong;Choi, Jung-Do
    • BMB Reports
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    • v.29 no.4
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    • pp.321-326
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    • 1996
  • Spinach glycolate oxidase was subjected to a series of chemical modifications aimed at identifying amino acid residues essential for catalytic activity. The oxidase was reversibly inactivated by treatment with pyridoxal 5'-phosphate (PLP). The inactivation by PLP was accompanied by the appearance of an absorption peak of around 430 nm, which was shifted to 325 nm upon reduction with $NaBH_4$. After reduction, the PLP-treated oxidase showed a fluorescence spectrum with a maximum of around 395 nm by exciting at 325 nm. The substrate-competitive inhibitors oxalate and oxaloacetate provided protection against inactivation of the oxidase by PLP. These results suggest that PLP inactivates the enzyme by fonning a Schiff base with lysyl residue(s) at an active site of the oxidase. The enzyme was also inactivated by tryptophan-specific reagent N-bromosuccinimide (NBS). However, competitive inhibitors oxalate and oxaloacetate could not protect the oxidase significantly against inactivation of the enzyme by NBS. The results implicate that the inactivation of the oxidase by NBS is not directly related to modification of the tryptophanyl residue at an active site of the enzyme. Treatments of the oxidase with cysteine-specific reagents iodoacetate, silver nitrate, and 5,5'-dithiobis-2-nitrobenzoic acid did not affect significantly the activity of the enzyme.

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Studies on $CO_2$-Fixation Ability and Photorespiration in Ginseng Leaves (인삼 잎의 $CO_2$ 고정능과 광호흡에 관한 연구)

  • 이인철
    • Journal of Plant Biology
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    • v.25 no.3
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    • pp.105-111
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    • 1982
  • These studies were undertaken to elucidate the reasons for the low productivity of ginseng by comparing the rate of $CO_2$-fixation and photorespiration, variation in the amounts of intermediates and enzyme activities of glycolate oxidase and catalase in ginseng with those of potato. The ability of $CO_2$-fixation in ginseng was found to be one half of that of potato and there were significant differences between those two plants in the rate of $^{14}C$ incorporated into glutamate, aspartate, malate and 3-PGA, but little differences in P-glycolate, glycolate, serine and glycine. The ratio of photorespiration to dark respiration and the activities of glycolate oxidase and catalase in the two species were about same, but ginseng showed higher ratio in photorespiration to total $CO_2$-fixation than potato did. These results indicated that the low productivity of ginseng may resulted from the low $CO_2$-fixation ability and high rate of photorespiration.

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$CO_2$ Evolution in Peroxisomes Isolated from Spinach Leaves at Various Ages (시금치 잎의 엽영에 따라 분리한 Peroxisome에서의$CO_2$방출)

  • 이순희
    • Journal of Plant Biology
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    • v.31 no.3
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    • pp.197-203
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    • 1988
  • The rates of photorespiration and total CO2 fixation depending on leaf ages of spinach (Spinacia oleracea L.) were investigated. Metabolic rates of glycolate and glyoxylate in isolated peroxisomes were also measured. The rate of photorespiration and total CO2 fixation ability increased with the maturing of leaf, but decreased with senescence. Activities of enzymes involved in the peroxisomal photorespiratory pathway such as catalase, glycolate oxidase, NADH-glyoxylate reductase and glutamate-glyoxylate transaminase were highest in the mature leaf, but also decreased with aging of leaf. Glutamate-glyxolate transaminase activity significantly decreased with senescence, especially. the metabolic rate of glycolate was observed to be lower than that of glyoxylate in isolated peroxisomes. Glycolate seemed to be metabolized mainly to glycine, however, it also oxidized to CO2 when glycolate was supplied as a substrate for glycine synthesis instead of glyoxylate. The conversion rates of glycolate and glyxylate into CO2 increased with the senescence of leaves.

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Effect of Light Quality on the Photorespiration in Pisum sativum L. (완두에서 광호흡에 미치는 광질의 영향)

  • 이순희
    • Journal of Plant Biology
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    • v.33 no.3
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    • pp.203-210
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    • 1990
  • Effects of blue and red light on photorespiration in the leaf disks of pea were studied. The rate of total 14CO2 fixation was more or less higher under red light than blue light irradiation of the same quantum (94.8 $\mu$Em-2.S-1/mV). The release of 14CO2 by photorespiration was more stimulated under blue than red light. Among the photorespiratory intermediates, 14C was more incorporated ito serine under blue light than red light. However, 14C was more incorporated into glycine under red light than blue light. The incorporation of 14C into glycolate was very low under both light qualities, but higher under red light than blue light. Among the enzymes related to photorespiration, only glycolate oxidase was activated and/or synthesized by blue light irradiation. Moreover, more 14C2 was released from glycoate-1-14C under blue light than red light irradiation, but 14C2 release from glyoxylate-1-14C and glycine-1-14C showed no difference by the either light qualities. These results suggest that blue light is more effective in the photorespiratory CO2 evolution than red light. The reason is considered that glycolate is easily metabolized under blue light due to the stimulation of the glycolate oxidase activity.

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Chemical Modification of Glycolate Oxidase from Spinach by Diethyl Pyrocarbonate. Evidence of Essential Histidine for Enzyme Activity$^\dag$

  • Lee, Kun-Kook;Kim, Hong-Sun;Choi, Jung-Do
    • Bulletin of the Korean Chemical Society
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    • v.8 no.4
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    • pp.280-285
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    • 1987
  • FMN-dependent glycolate oxidase from spinach is inactivated by diethyl pyrocarbonate at pH 7.0. Inactivation of both apo- and holoenzyme by diethyl pyrocarbonate follows pseudo-first-order kinetics and first order with respect to the reagent. A series of difference spectra of inactivated and native enzymes show a single peak at 240 nm, indicating the modification of histidyl residues. No decrease in absorbance at around 280 nm due to formation of O-carbethoxytyrosine is observed. The rate of inactivation is dependent on pH, and the data for pH dependent rates implicate the involvement of a group with a pKa of 6.9. The activity lost by treatment with diethyl pyrocarbonate could be almost fully restored by incubation with 0.75M hydroxylamine. The reactivation by hydroxylamine and the pH dependence of inactivation are also consistent with that the inactivation is due to modification of histidyl residues. Although coenzyme FMN is without protective effect, the substrate glycolate, the product glyoxylate, and two competitive inhibitors, oxalate and oxalacetate, provide marked protection against the inactivation of the holoenzyme. These results suggest that the inactivation of the oxidase by diethyl pyrocarbonate occurs by modification of essential histidyl residue(s) at the active site.

Isolation and Characterization of Glycolate Oxidase Gene from Panax ginseng C. A. Meyer

  • Parvin, Shohana;Pulla, Rama Krishna;Kim, Yu-Jin;Sathiyaraj, Gayathri;Jung, Seok-Kyu;Khorolragchaa, Altanzul;In, Jun-Gyo;Yang, Deok-Chun
    • Journal of Ginseng Research
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    • v.33 no.4
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    • pp.249-255
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    • 2009
  • The oxidation of glycolate to glyoxylate, a key step in plant photorespiration, is carried out by the peroxisomal flavoprotein glycolate oxidase (EC 1.1.3.15). To investigate the altered gene expression and the role of GOX in ginseng plant defense system, a cDNA clone containing a GOX gene designated as PgGOX was isolated and sequenced from Panax ginseng. The cDNA was 692 nucleotides long and have an open reading frame of 552 bp with a deduced amino acid sequence of 183 residues. A GenBank BlastX search revealed that the deduced amino acid of PgGOX shares a high degree homology with the Glycine max (95% identity). In the present study we analyzed the expression of PgGOX under various environmental stresses at different times using real time-PCR. The results showed that the expressions of PgGOX increased after various treatments involving salt, light, cold, ABA, SA, and copper treatment.

Changes in the Activities of Certain Enzymes in Tobacco Leaf (Nicotiana tabacum) during Growth (연초엽조직의 물질대사에 관여하는 몇가지 효소활성에 관하여)

  • 김준철;윤경은;강서규
    • Journal of the Korean Society of Tobacco Science
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    • v.4 no.1
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    • pp.1-5
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    • 1982
  • The metabolic enzymes, nitrate reductase, amylase and peroxidase and the Photorespiratory enzyme, Slycolate oxidise in Nicotiana tabacum varieties were studied at various growth stages. The enzyme activities of young leaves with rapid growth were different from those of old ones with stationary growth. In young leaves, activity of nitrate reductase was higher than that in mature ones and amylase activity was fairly constant in all stages. Activities of glycolate oxidise and peroxidase were found to be significantly lower in young leaves than in mature ones. Activity of glycolate oxidase in mature middle leaves was 2.45 times higher than that of young ones and inhibited by 36% when the enzyme was treated with 0.16 mM isonicotinic hydrazide.

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Effects of Nitrogen Sources on Chlorophyll, and Oxidases in Soybean Leaves different in Phosphorus Sensitivity (인산감수성(燐酸感受性)이 다른 대두엽(大豆葉)의 엽록소(葉綠素) 및 산화효소(酸化酵素)에 대(對)한 질소원(窒素源)의 영향(影響))

  • Park, Hoon;Stutte, Charles A.
    • Korean Journal of Soil Science and Fertilizer
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    • v.6 no.3
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    • pp.185-191
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    • 1973
  • Effects of nitrogen sources on chlorophyll, activity of some oxidases in soybean leaves were investigated in relation to phosphorus sensitivity. Ammonium and urea culture accelerated leaf senescence more in phosphorus sensitive cultivars. The leaf senescence patterns affected by nitrogen sources were clearly indicated by intact leaf absorbance. Absorption maximum (670nm in methanol extraction or 685nm in intact leaf), was not changed by nitrogen source in the same method. According to leaf senesence pattern general physiological sensitivity pattern was discussed. IAA-oxidase activity was higher in the phosphorus tolerant cultivars and nitrate treatment than in the sensitive cultivars and ammonium treatment. Glycolate oxidase activity was higher in the sensitive cultivars and nitrate treatment. Polyphenol oxidase activity was higher in the tolerant cultivars and urea treatment. It is concluded that the excess ammonium, to which excess phosphorus is highly similar in physiological effect, disturbs the photosynthetic system by inhibition of ATP generation (photo-and oxidative phosphorylation).

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