1887

Abstract

Summary: Glutamine synthetase (EC 6.3.1.2) was purified about 430-fold from the nitrifying bacterium by affinity chromatography on Blue Sepharose CL-6B and gel filtration on Sepharose 4B. The enzyme (apparent mol. wt 700000), which consisted of 12 subunits, each of mol. wt 58000, required a divalent cation for both biosynthetic and transferase activities. Regulation of glutamine synthetase both by a feedback inhibition involving amino acids and by an adenylylation/deadenylylation mechanism was studied. The enzyme was highly adenylylated (75-90%) in cell free extracts from cells grown on nitrite as the sole source of nitrogen. The adenylylated form of the enzyme could be deadenylylated by treatment with snake venom phos-phodiesterase. An isoactivity pH of 7·4 was recorded for glutamine synthetase.

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/content/journal/micro/10.1099/00221287-130-4-959
1984-04-01
2020-01-26
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-130-4-959
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