Adenosine triphosphate: glutamine synthetase adenylyltransferase of Escherichia coli: two active molecular forms.
Two active forms of purified ATP:glutamine synthetase adenylyl-transferase from Escherichia coli are apparent on polyacrylamide gel electrophoresis at pH 8. The slower migrating component, which is identical to the P(I)-protein fraction of the glutamine synthetase deadenylylating enzyme system, has S(20.w) congruent with 5.1 S and a molecular weight of about 130,000. The more rapidly migrating adenylyltransferase component has S(20.w) congruent with 4.0 S and a molecular weight of about 70,000. During storage at 4 degrees C, the larger adenylyltransferase component (P(I)) converts to the smaller active unit with a concomitant loss of both P(I) deadenylylating activity and soluble protein. It is concluded that the low-molecular weight form of the adenylyltransferase is a subunit of the deadenylylating P(I)-protein.
D000227:Adenine Nucleotides; D000255:Adenosine Triphosphate; D001426:Bacterial Proteins / Q000032:analysis; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D004926:Escherichia coli / Q000201:enzymology*; D005973:Glutamine; D006358:Hot Temperature; D006882:Hydroxyapatites; D007527:Isoenzymes / Q000032:analysis*; D008025:Ligases; D008970:Molecular Weight; D009713:Nucleotidyltransferases / Q000032:analysis* / Q000037:antagonists & inhibitors; D013451:Sulfonic Acids
D000227:Adenine Nucleotides; D001426:Bacterial Proteins; D006882:Hydroxyapatites; D007527:Isoenzymes; D013451:Sulfonic Acids; D005973:Glutamine; D000255:Adenosine Triphosphate; D009713:Nucleotidyltransferases; D008025:Ligases