Relation between the adenylylation state of glutamine synthetase and the expression of other genes involved in nitrogen metabolism.
We have partially characterized the biochemical parameters of glutamine synthetase from Klebsiella pneumoniae and have shown that the differential affinity of adenylylated and unadenylylated glutamine synthetase for adenosine diphosphate provides a convenient means of determining the adenylylation state. Using this assay procedure, we examined the relationship between the adenylylation state and the expression of other genes involved in nitrogen assimilation. We observed no correlation between the adenylylation state and the expression of histidase, glutamine synthetase, glutamate synthase, glutamate dehydrogenase, and urease in aerobic cultures.
D000244:Adenosine Diphosphate / Q000378:metabolism*; D000332:Aerobiosis; D000642:Ammonia-Lyases / Q000096:biosynthesis*; D000693:Anaerobiosis; D005969:Glutamate Dehydrogenase / Q000096:biosynthesis*; D005970:Glutamate Synthase / Q000096:biosynthesis*; D005974:Glutamate-Ammonia Ligase / Q000096:biosynthesis / Q000378:metabolism*; D006638:Histidine Ammonia-Lyase / Q000096:biosynthesis*; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D000637:Transaminases / Q000096:biosynthesis*; D014510:Urease / Q000096:biosynthesis*; D001616:beta-Galactosidase / Q000096:biosynthesis
D000244:Adenosine Diphosphate; D005970:Glutamate Synthase; D005969:Glutamate Dehydrogenase; D000637:Transaminases; D001616:beta-Galactosidase; D014510:Urease; D000642:Ammonia-Lyases; D006638:Histidine Ammonia-Lyase; D005974:Glutamate-Ammonia Ligase