Disease relevance of glnA

• In heterologous expression experiments, glnA2, glnA3, and glnA4, in contrast to glnA and glnII, were not capable of complementing the L: -glutamine auxotrophy of an Escherichia coli glnA mutant [1].
• The poor growth of Rhodospirillum rubrum mutants lacking PII proteins is due to an excess of glutamine synthetase activity [2].
• Investigation of the functional properties and regulation of three glutamine synthetase-like genes in Streptomyces coelicolor A3(2) [1].

High impact information on glnA

• The result underscores the importance of proper regulation of GS activity for cell growth [2].
• All of these results strongly imply that elevated GS activity is the causative basis for the poor growth seen in R. rubrum mutants lacking P(II) and presumably in mutants of some other organisms with similar genotypes [2].
• Escherichia coli Glutamine Synthetase Adenylyltransferase (ATase, EC 2.7.7.49): Kinetic Characterization of Regulation by PII, PII-UMP, Glutamine, and alpha-Ketoglutarate [3].
• Stereochemistry of binding of thiophosphate analogs of ATP and ADP to carbamate kinase, glutamine synthetase, and carbamoyl-phosphate synthetase [4].
• An alternative pathway involves the combined activities of glutamine synthetase, which aminates glutamate to form glutamine, and glutamate synthase, which transfers the amide group of glutamine to 2-oxoglutarate to yield two molecules of glutamate [5].

Associations of glnA with chemical compounds

• Molecular analysis of two mutants from Lotus japonicus deficient in plastidic glutamine synthetase: functional properties of purified GLN2 enzymes [6].

References