Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis
Kinetic analysis of glyceraldehyde-3-phosphate dehydrogenase showed that the enhancement of the NADP-linked activity by specific chloroplast modulators is a concerted process; either a selected second metabolite or the couple dithiothreitol/thioredoxin-f lowers the concentration of primary modulator...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00039861_v246_n1_p1_Wolosiuk |
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todo:paper_00039861_v246_n1_p1_Wolosiuk2023-10-03T13:57:00Z Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis Wolosiuk, R.A. Hertig, C.M. Busconi, L. adenosine triphosphate alcohol derivative dithiothreitol glyceraldehyde 3 phosphate dehydrogenase Glyceraldehyde 3 Phosphate Dehydrogenases nicotinamide adenine dinucleotide phosphate phosphate propanol solvent spermine thioredoxin f vegetable protein article chloroplast drug effect enzyme activation enzymology metabolism plant 1-Propanol Adenosine Triphosphate Alcohols Chloroplasts Dithiothreitol Enzyme Activation Glyceraldehyde-3-Phosphate Dehydrogenases NADP Phosphates Plant Proteins Plants Solvents Spermine Kinetic analysis of glyceraldehyde-3-phosphate dehydrogenase showed that the enhancement of the NADP-linked activity by specific chloroplast modulators is a concerted process; either a selected second metabolite or the couple dithiothreitol/thioredoxin-f lowers the concentration of primary modulators (ATP, NADPH, inorganic phosphate, 1,3-diphosphoglycerate) required for maximal stimulation (A0.5). Organic solvents also stimulate NADP-glyceraldehyde-3-phosphate dehydrogenase in the absence of any modulator; the concentration for the highest specific activity correlates inversely with the respective octanol-water partition coefficient. On the other hand, alcohols also enhance enzyme activity by lowering the A0.5 for primary modulators. Another compound-spermine-inhibits both the ATP- and the inorganic phosphate-mediated activation, but it does not influence the NADPH-induced process. © 1986. Fil:Wolosiuk, R.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Hertig, C.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Busconi, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00039861_v246_n1_p1_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 |
adenosine triphosphate alcohol derivative dithiothreitol glyceraldehyde 3 phosphate dehydrogenase Glyceraldehyde 3 Phosphate Dehydrogenases nicotinamide adenine dinucleotide phosphate phosphate propanol solvent spermine thioredoxin f vegetable protein article chloroplast drug effect enzyme activation enzymology metabolism plant 1-Propanol Adenosine Triphosphate Alcohols Chloroplasts Dithiothreitol Enzyme Activation Glyceraldehyde-3-Phosphate Dehydrogenases NADP Phosphates Plant Proteins Plants Solvents Spermine |
| spellingShingle |
adenosine triphosphate alcohol derivative dithiothreitol glyceraldehyde 3 phosphate dehydrogenase Glyceraldehyde 3 Phosphate Dehydrogenases nicotinamide adenine dinucleotide phosphate phosphate propanol solvent spermine thioredoxin f vegetable protein article chloroplast drug effect enzyme activation enzymology metabolism plant 1-Propanol Adenosine Triphosphate Alcohols Chloroplasts Dithiothreitol Enzyme Activation Glyceraldehyde-3-Phosphate Dehydrogenases NADP Phosphates Plant Proteins Plants Solvents Spermine Wolosiuk, R.A. Hertig, C.M. Busconi, L. Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis |
| topic_facet |
adenosine triphosphate alcohol derivative dithiothreitol glyceraldehyde 3 phosphate dehydrogenase Glyceraldehyde 3 Phosphate Dehydrogenases nicotinamide adenine dinucleotide phosphate phosphate propanol solvent spermine thioredoxin f vegetable protein article chloroplast drug effect enzyme activation enzymology metabolism plant 1-Propanol Adenosine Triphosphate Alcohols Chloroplasts Dithiothreitol Enzyme Activation Glyceraldehyde-3-Phosphate Dehydrogenases NADP Phosphates Plant Proteins Plants Solvents Spermine |
| description |
Kinetic analysis of glyceraldehyde-3-phosphate dehydrogenase showed that the enhancement of the NADP-linked activity by specific chloroplast modulators is a concerted process; either a selected second metabolite or the couple dithiothreitol/thioredoxin-f lowers the concentration of primary modulators (ATP, NADPH, inorganic phosphate, 1,3-diphosphoglycerate) required for maximal stimulation (A0.5). Organic solvents also stimulate NADP-glyceraldehyde-3-phosphate dehydrogenase in the absence of any modulator; the concentration for the highest specific activity correlates inversely with the respective octanol-water partition coefficient. On the other hand, alcohols also enhance enzyme activity by lowering the A0.5 for primary modulators. Another compound-spermine-inhibits both the ATP- and the inorganic phosphate-mediated activation, but it does not influence the NADPH-induced process. © 1986. |
| format |
JOUR |
| author |
Wolosiuk, R.A. Hertig, C.M. Busconi, L. |
| author_facet |
Wolosiuk, R.A. Hertig, C.M. Busconi, L. |
| author_sort |
Wolosiuk, R.A. |
| title |
Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis |
| title_short |
Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis |
| title_full |
Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis |
| title_fullStr |
Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis |
| title_full_unstemmed |
Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis |
| title_sort |
activation of spinach chloroplast nadp-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis |
| url |
http://hdl.handle.net/20.500.12110/paper_00039861_v246_n1_p1_Wolosiuk |
| work_keys_str_mv |
AT wolosiukra activationofspinachchloroplastnadplinkedglyceraldehyde3phosphatedehydrogenasebyconcertedhysteresis AT hertigcm activationofspinachchloroplastnadplinkedglyceraldehyde3phosphatedehydrogenasebyconcertedhysteresis AT busconil activationofspinachchloroplastnadplinkedglyceraldehyde3phosphatedehydrogenasebyconcertedhysteresis |
| _version_ |
1807323572315619328 |