Primary Structure of Escherichia coli Glutamine Synthetase

Mn2+ and substrate interactions with glutamine synthetase from Escherichia coli.

Regulation of glutamine synthetase. X. Effect of growth conditions on the susceptibility of Escherichia coli glutamine synthetase to feedback inhibition.

The kinetic properties of Escherichia coli glutamine synthetase are markedly influenced by the manner in which the organism is grown. Enzyme obtained from stationary-phase cells grown on glycerol and glutamate is strongely inhibited by each of the eight feedback effectors known to influence this enzyme; however, the enzyme from log-phase cells grown on glucose and growth-limiting concentrations...

Primary structure of CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) from Escherichia coli.

The gene coding for CTP:CMP-3-deoxy-D-mannooctulosonate cytidylyltransferase (CMP-KDO synthetase), kds B, was previously cloned on a 9-kilobase Pst insert of Escherichia coli DNA into pBR 322 (Goldman, R. C., and Kohlbrenner, W. E. (1985) J. Bacteriol. 163, 256-261). Using a transposon mutagenesis approach we have now located kds B on this insert, which facilitated the isolation and sequencing ...

Scanning transmission electron microscopy of submolecular oligomers of stabilized glutamine synthetase from Escherichia coli.

Stabilized Escherichia coli glutamine synthetase subparticles fractionated by high pressure liquid chromatography gel fitration as described in the text were examined by scanning transmission electron microscopy using the Brookhaven Scanning Transmission Electron Microscopy Resource Facility. The operating characteristics of this microscope have been previously published (1). Samples were negat...

Reversible adenylylation of glutamine synthetase is dynamically counterbalanced during steady-state growth of Escherichia coli.

Glutamine synthetase (GS) is the central enzyme for nitrogen assimilation in Escherichia coli and is subject to reversible adenylylation (inactivation) by a bifunctional GS adenylyltransferase/adenylyl-removing enzyme (ATase). In vitro, both of the opposing activities of ATase are regulated by small effectors, most notably glutamine and 2-oxoglutarate. In vivo, adenylyltransferase (AT) activity...