Studies on the regulation of chloroplast fructose-1,6-bisphosphatase. Activation by fructose 1,6-bisphosphate
Chloroplast fructose-1,6-bisphosphatase d-fructose 1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) isolated from spinach leaves, was activated by preincubation with fructose 1,6-bisphosphate. The rate of activation was slower than the rate of catalysis, and dependent upon the temperature and the c...
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1980
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v613_n2_p429_Chehebar http://hdl.handle.net/20.500.12110/paper_00052744_v613_n2_p429_Chehebar |
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paper:paper_00052744_v613_n2_p429_Chehebar2023-06-08T14:29:56Z Studies on the regulation of chloroplast fructose-1,6-bisphosphatase. Activation by fructose 1,6-bisphosphate (Chloroplast) Activation Fructose 1,6-bisphosphate Fructose-1,6-bisphosphatase Regulation fructose bisphosphatase fructose bisphosphate hexose phosphate article chloroplast drug effect enzyme activation enzymology kinetics metabolism plant Chloroplasts Enzyme Activation Fructose-Bisphosphatase Fructosediphosphates Hexosediphosphates Kinetics Plants Chloroplast fructose-1,6-bisphosphatase d-fructose 1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) isolated from spinach leaves, was activated by preincubation with fructose 1,6-bisphosphate. The rate of activation was slower than the rate of catalysis, and dependent upon the temperature and the concentration of fructose 1,6-bisphosphate. The addition of other sugar diphosphates, sugar monophosphates or intermediates of the reductive pentose phosphate cycle neither replaced fructose 1,6-bisphosphate nor modified the activation process. Upon activation with the effector the enzyme was less sensitive to trypsin digestion and insensitive to mercurials. The activity of chloroplast fructose-1,6-bisphosphatase, preincubated with fructose 1,6-bisphosphate, returned to its basal activity after the concentration of the effector was lowered in the preincubation mixture. The results provide evidence that fructose-1,6-bisophosphatase resembles other regulatory enzymes involved in photosynthetic CO2 assimilation in its activation by chloroplast metabolites. © 1980. 1980 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v613_n2_p429_Chehebar http://hdl.handle.net/20.500.12110/paper_00052744_v613_n2_p429_Chehebar |
| 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) Activation Fructose 1,6-bisphosphate Fructose-1,6-bisphosphatase Regulation fructose bisphosphatase fructose bisphosphate hexose phosphate article chloroplast drug effect enzyme activation enzymology kinetics metabolism plant Chloroplasts Enzyme Activation Fructose-Bisphosphatase Fructosediphosphates Hexosediphosphates Kinetics Plants |
| spellingShingle |
(Chloroplast) Activation Fructose 1,6-bisphosphate Fructose-1,6-bisphosphatase Regulation fructose bisphosphatase fructose bisphosphate hexose phosphate article chloroplast drug effect enzyme activation enzymology kinetics metabolism plant Chloroplasts Enzyme Activation Fructose-Bisphosphatase Fructosediphosphates Hexosediphosphates Kinetics Plants Studies on the regulation of chloroplast fructose-1,6-bisphosphatase. Activation by fructose 1,6-bisphosphate |
| topic_facet |
(Chloroplast) Activation Fructose 1,6-bisphosphate Fructose-1,6-bisphosphatase Regulation fructose bisphosphatase fructose bisphosphate hexose phosphate article chloroplast drug effect enzyme activation enzymology kinetics metabolism plant Chloroplasts Enzyme Activation Fructose-Bisphosphatase Fructosediphosphates Hexosediphosphates Kinetics Plants |
| description |
Chloroplast fructose-1,6-bisphosphatase d-fructose 1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) isolated from spinach leaves, was activated by preincubation with fructose 1,6-bisphosphate. The rate of activation was slower than the rate of catalysis, and dependent upon the temperature and the concentration of fructose 1,6-bisphosphate. The addition of other sugar diphosphates, sugar monophosphates or intermediates of the reductive pentose phosphate cycle neither replaced fructose 1,6-bisphosphate nor modified the activation process. Upon activation with the effector the enzyme was less sensitive to trypsin digestion and insensitive to mercurials. The activity of chloroplast fructose-1,6-bisphosphatase, preincubated with fructose 1,6-bisphosphate, returned to its basal activity after the concentration of the effector was lowered in the preincubation mixture. The results provide evidence that fructose-1,6-bisophosphatase resembles other regulatory enzymes involved in photosynthetic CO2 assimilation in its activation by chloroplast metabolites. © 1980. |
| title |
Studies on the regulation of chloroplast fructose-1,6-bisphosphatase. Activation by fructose 1,6-bisphosphate |
| title_short |
Studies on the regulation of chloroplast fructose-1,6-bisphosphatase. Activation by fructose 1,6-bisphosphate |
| title_full |
Studies on the regulation of chloroplast fructose-1,6-bisphosphatase. Activation by fructose 1,6-bisphosphate |
| title_fullStr |
Studies on the regulation of chloroplast fructose-1,6-bisphosphatase. Activation by fructose 1,6-bisphosphate |
| title_full_unstemmed |
Studies on the regulation of chloroplast fructose-1,6-bisphosphatase. Activation by fructose 1,6-bisphosphate |
| title_sort |
studies on the regulation of chloroplast fructose-1,6-bisphosphatase. activation by fructose 1,6-bisphosphate |
| publishDate |
1980 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052744_v613_n2_p429_Chehebar http://hdl.handle.net/20.500.12110/paper_00052744_v613_n2_p429_Chehebar |
| _version_ |
1768542816299909120 |