Dual effects of organic solvents on chloroplast phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase
Organic solvents miscible in water (cosolvents) exerted a dual effect on the activation stage of two thioredoxin-linked enzymes of the reductive pentose phosphate cycle, phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase, both from spinach chloroplast; the enzyme specific activity was sti...
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1985
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paper:paper_00145793_v189_n2_p212_Wolosiuk2023-06-08T14:37:31Z Dual effects of organic solvents on chloroplast phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase Wolosiuk, Ricardo Alejandro Chloroplast enzyme Enzyme activation tPhotosynthesis NADP-glyceraldehyde-3-phosphate dehydrogenase Organic solvent Phosphoribulokinase organic solvent phosphoribulokinase chloroplast enzyme activation higher plant nicotinamide adenine dinucleotide phosphate glyceraldehyde 3 phosphate dehydrogenase nonhuman photosynthesis priority journal Organic solvents miscible in water (cosolvents) exerted a dual effect on the activation stage of two thioredoxin-linked enzymes of the reductive pentose phosphate cycle, phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase, both from spinach chloroplast; the enzyme specific activity was stimulated and inhibited by low and high concentrations of alcohols, respectively. On the contrary, cosolvents inhibited the catalytic process. In the stimulation of phosphoribulokinase activation, organic solvents reduced the requirement for thioredoxin-f and changed the thiol specificity, so that monothiols became functional. The cosolvent-mediated enhancement of NADP-glyceraldehyde-3-P dehydrogenase was obtained in the absence of modulators. With both enzymes, the concentration of the organic solvents required for activation was inversely proportional to its hydrophobicity (1-butanol < 1-propanol < 2-propanol < ethanol). The present results demonstrate the participation of a new component, the enzyme microenvironment, in the regulation of thioredoxin-linked chloroplast enzymes. © 1985. Fil:Wolosiuk, R.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1985 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v189_n2_p212_Wolosiuk http://hdl.handle.net/20.500.12110/paper_00145793_v189_n2_p212_Wolosiuk |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Chloroplast enzyme Enzyme activation tPhotosynthesis NADP-glyceraldehyde-3-phosphate dehydrogenase Organic solvent Phosphoribulokinase organic solvent phosphoribulokinase chloroplast enzyme activation higher plant nicotinamide adenine dinucleotide phosphate glyceraldehyde 3 phosphate dehydrogenase nonhuman photosynthesis priority journal |
| spellingShingle |
Chloroplast enzyme Enzyme activation tPhotosynthesis NADP-glyceraldehyde-3-phosphate dehydrogenase Organic solvent Phosphoribulokinase organic solvent phosphoribulokinase chloroplast enzyme activation higher plant nicotinamide adenine dinucleotide phosphate glyceraldehyde 3 phosphate dehydrogenase nonhuman photosynthesis priority journal Wolosiuk, Ricardo Alejandro Dual effects of organic solvents on chloroplast phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase |
| topic_facet |
Chloroplast enzyme Enzyme activation tPhotosynthesis NADP-glyceraldehyde-3-phosphate dehydrogenase Organic solvent Phosphoribulokinase organic solvent phosphoribulokinase chloroplast enzyme activation higher plant nicotinamide adenine dinucleotide phosphate glyceraldehyde 3 phosphate dehydrogenase nonhuman photosynthesis priority journal |
| description |
Organic solvents miscible in water (cosolvents) exerted a dual effect on the activation stage of two thioredoxin-linked enzymes of the reductive pentose phosphate cycle, phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase, both from spinach chloroplast; the enzyme specific activity was stimulated and inhibited by low and high concentrations of alcohols, respectively. On the contrary, cosolvents inhibited the catalytic process. In the stimulation of phosphoribulokinase activation, organic solvents reduced the requirement for thioredoxin-f and changed the thiol specificity, so that monothiols became functional. The cosolvent-mediated enhancement of NADP-glyceraldehyde-3-P dehydrogenase was obtained in the absence of modulators. With both enzymes, the concentration of the organic solvents required for activation was inversely proportional to its hydrophobicity (1-butanol < 1-propanol < 2-propanol < ethanol). The present results demonstrate the participation of a new component, the enzyme microenvironment, in the regulation of thioredoxin-linked chloroplast enzymes. © 1985. |
| author |
Wolosiuk, Ricardo Alejandro |
| author_facet |
Wolosiuk, Ricardo Alejandro |
| author_sort |
Wolosiuk, Ricardo Alejandro |
| title |
Dual effects of organic solvents on chloroplast phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase |
| title_short |
Dual effects of organic solvents on chloroplast phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase |
| title_full |
Dual effects of organic solvents on chloroplast phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase |
| title_fullStr |
Dual effects of organic solvents on chloroplast phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase |
| title_full_unstemmed |
Dual effects of organic solvents on chloroplast phosphoribulokinase and NADP-glyceraldehyde-3-P dehydrogenase |
| title_sort |
dual effects of organic solvents on chloroplast phosphoribulokinase and nadp-glyceraldehyde-3-p dehydrogenase |
| publishDate |
1985 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v189_n2_p212_Wolosiuk http://hdl.handle.net/20.500.12110/paper_00145793_v189_n2_p212_Wolosiuk |
| work_keys_str_mv |
AT wolosiukricardoalejandro dualeffectsoforganicsolventsonchloroplastphosphoribulokinaseandnadpglyceraldehyde3pdehydrogenase |
| _version_ |
1768546098035556352 |