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• W2082014489 abstract "Abstract Two isoenzymes of glutamine synthetase (EC 6.3.1.2), GS 1 and GS 2 , have been purified from cells of Emiliania huxleyi using Cibacron blue dye ligand chromatography and gel filtration, separated by ion-exchange chromatography on Mono-Q and partly characterized. Each enzyme is a homohexamer with a molecular mass of 402 kDa for GS 1 and 501 kDa for GS 2 . The molecular mass of the subunits of GS 1 and GS 2 was estimated to be 61 and 78 kDa, respectively. As in higher plants, GS 1 is slightly more thermostable than GS 2 and much less stimulated by thiols than GS 2 . For these reasons, GS 1 was designated as the cytosolic enzyme and GS 2 as the chloroplastic one. Although the K m s for NH 2 OH are about the same, GS 2 possesses a much higher affinity for glutamine than GS 1 . As in bacteria, ATP appears to play an important role in the allosteric regulation of GS 2 . l -Ala and CTP are potent inhibitors of GS 1 activity. CTP, carbamoyl-phosphate and l -Ala exert a cumulative inhibitory effect on GS 1 activity. GS 2 is also inhibited to some extent by l -Ala and l -His. NH 2 -terminal sequence analysis of GS 2 did not show any homology with bacteria, cyanobacteria or higher plants." @default.
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• W2082014489 date "1997-12-01" @default.
• W2082014489 modified "2023-10-16" @default.
• W2082014489 title "Isoforms of Glutamine Synthetase in the Marine Coccolithophorid Emiliania huxleyi (Prymnesiophyceae)" @default.
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• W2082014489 doi "https://doi.org/10.1016/s0305-0491(97)00279-4" @default.
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