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Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems

Identifieur interne : 00DF88 ( Main/Exploration ); précédent : 00DF87; suivant : 00DF89

Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems

Auteurs : F. Rebeille [France] ; M. D. Hatch [Australie]

Source :

Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1986.

RBID : ISTEX:13845390E7062D4A95C626A0BE88513D5D0742F8

Descripteurs français

Wicri :
- topic : Maïs.

English descriptors

KwdEn :
- Assay, Biochem, Biophys, Chloroplast, Dehydrogenase, Dhap, Edta, Electron flux, Enzyme activity, Ferredoxin, Final concentration, Final concentrations, High ratios, Inactivation, Initial rate, Intact chloroplasts, Light intensity, Maize, Mesophyll, Mesophyll chloroplasts, Nadp, Nadp ratio, Nadp ratios, Nadph, Nadph concentration, Nadpmdh, Oxidized, Oxidized thioredoxin, Photosynthesis, Photosynthetic metabolites, Present studies, Pyridine nucleotide, Redox, Redox state, Reduceable, Reduceable substrates, Thiol groups, Thioredoxin, Thioredoxin content, Thioredoxin redox state, Total amount.
Teeft :
- Assay, Biochem, Biophys, Chloroplast, Dehydrogenase, Dhap, Edta, Electron flux, Enzyme activity, Ferredoxin, Final concentration, Final concentrations, High ratios, Inactivation, Initial rate, Intact chloroplasts, Light intensity, Maize, Mesophyll, Mesophyll chloroplasts, Nadp, Nadp ratio, Nadp ratios, Nadph, Nadph concentration, Nadpmdh, Oxidized, Oxidized thioredoxin, Photosynthesis, Photosynthetic metabolites, Present studies, Pyridine nucleotide, Redox, Redox state, Reduceable, Reduceable substrates, Thiol groups, Thioredoxin, Thioredoxin content, Thioredoxin redox state, Total amount.

Abstract

Abstract: Activation and inactivation of NADP-malate dehydrogenase purified from Zea mays leaves were followed in a reconstituted system provided with thioredoxin poised in various redox states with dithiothreitol. The initial rate of activation or inactivation of NADP-malate dehydrogenase was proportional to the concentration of reduced or oxidized thioredoxin, respectively. The rate of inactivation was about 16 times that for activation at pH 7.4. Both activities increased when the pH was increased from 7.4 to 8.0. The redox potentials (E′0, pH 7) for the dithiol-disulfide systems of thioredoxin and NADP-malate dehydrogenase were estimated to be about −0.30 and −0.33 V, respectively. As would be predicted from these values, high proportions of active malate dehydrogenase were developed only in the presence of very high ratios of reduced to oxidized thioredoxin. Similarly, when pyridine nucleotide was included, a high degree of activation of malate dehydrogenase was only observed with high NADPHNADP ratios. These results confirm predictions based on models developed in earlier studies that the NADPH to NADP ratio as well as the thioredoxin redox state may be critical in determining the level of NADP-malate dehydrogenase activity in vivo.

Url:

DOI: 10.1016/0003-9861(86)90571-0

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">Abstract: Activation and inactivation of NADP-malate dehydrogenase purified from Zea mays leaves were followed in a reconstituted system provided with thioredoxin poised in various redox states with dithiothreitol. The initial rate of activation or inactivation of NADP-malate dehydrogenase was proportional to the concentration of reduced or oxidized thioredoxin, respectively. The rate of inactivation was about 16 times that for activation at pH 7.4. Both activities increased when the pH was increased from 7.4 to 8.0. The redox potentials (E′0, pH 7) for the dithiol-disulfide systems of thioredoxin and NADP-malate dehydrogenase were estimated to be about −0.30 and −0.33 V, respectively. As would be predicted from these values, high proportions of active malate dehydrogenase were developed only in the presence of very high ratios of reduced to oxidized thioredoxin. Similarly, when pyridine nucleotide was included, a high degree of activation of malate dehydrogenase was only observed with high NADPHNADP ratios. These results confirm predictions based on models developed in earlier studies that the NADPH to NADP ratio as well as the thioredoxin redox state may be critical in determining the level of NADP-malate dehydrogenase activity in vivo.</div>
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Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems

Regulation of NADP-malate dehydrogenase in C4 plants: Effect of varying NADPH to NADP ratios and thioredoxin redox state on enzyme activity in reconstituted systems

Source :

Descripteurs français

English descriptors

Abstract

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Le document en format XML

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