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Effect of some compounds on glutamine synthetase isoforms activity from triticale seedling leaves



Effect of some compounds on glutamine synthetase isoforms activity from triticale seedling leaves



Acta Physiologiae Plantarum 16(4): 303-308



The Mg-2+-dependent activity of the chloroplastic form of glutamine synthetase was activated by hydrosulphide compounds while the activity of the cytoplasmic form of the enzyme did not change under the same conditions. Moreover, the chloroplastic enzyme activity was much stronger inhibited by the inhibitors binding the enzyme SH groups than it happened in case of cytosolic one. Besides the compounds binding the enzyme SH groups, some bivalent metal ions (Mn-2+, Co-2+, Ca-2+) also affected the activity of both forms of glutamine synthetase (GS). Total substitution of the Mg-2+ With Mn-2+ or Co-2+ not only decreases the activity of both GS isoforms but also decreases their substrate specificity to L-glutamate and ATP. Both activities were also inhibited by the reduced forms of glutamate dehydrogenase coenzymes (NADH, NADPH) and such nucleotides as AMP, CTP and GTP.

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Accession: 002604665

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