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...
Guardado en:
| Autores principales: | , , |
|---|---|
| Publicado: |
1986
|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v246_n1_p1_Wolosiuk http://hdl.handle.net/20.500.12110/paper_00039861_v246_n1_p1_Wolosiuk |
| Aporte de: |
| id |
paper:paper_00039861_v246_n1_p1_Wolosiuk |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_00039861_v246_n1_p1_Wolosiuk2023-06-08T14:25:01Z Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis Wolosiuk, Ricardo Alejandro Hertig, Cecilia Margarita Busconi, Liliana 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. 1986 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v246_n1_p1_Wolosiuk 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, Ricardo Alejandro Hertig, Cecilia Margarita Busconi, Liliana 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. |
| author |
Wolosiuk, Ricardo Alejandro Hertig, Cecilia Margarita Busconi, Liliana |
| author_facet |
Wolosiuk, Ricardo Alejandro Hertig, Cecilia Margarita Busconi, Liliana |
| author_sort |
Wolosiuk, Ricardo Alejandro |
| 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 |
| publishDate |
1986 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v246_n1_p1_Wolosiuk http://hdl.handle.net/20.500.12110/paper_00039861_v246_n1_p1_Wolosiuk |
| work_keys_str_mv |
AT wolosiukricardoalejandro activationofspinachchloroplastnadplinkedglyceraldehyde3phosphatedehydrogenasebyconcertedhysteresis AT hertigceciliamargarita activationofspinachchloroplastnadplinkedglyceraldehyde3phosphatedehydrogenasebyconcertedhysteresis AT busconililiana activationofspinachchloroplastnadplinkedglyceraldehyde3phosphatedehydrogenasebyconcertedhysteresis |
| _version_ |
1768545905226547200 |