Allosteric regulation of the state of adenylylation of glutamine synthetase in permeabilized cell preparations of Escherichia coli. Studies of monocyclic and bicyclic interconvertible enzyme cascades, in situ.-Reference-Cited by-同舟云学术

Allosteric regulation of the state of adenylylation of glutamine synthetase in permeabilized cell preparations of Escherichia coli. Studies of monocyclic and bicyclic interconvertible enzyme cascades, in situ.

Published:1981-12 Issue:24 Volume:256 Page:13022-13029
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Mura U,Chock P.B.,Stadtman E.R.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference19 articles.

1. Modulation of Glutamine Synthetase Adenylylation and Deadenylylation Is Mediated by Metabolic Transformation of the PII-Regulatory Protein

2. Glutamine synthetase cascade: Enrichment of uridylyltransferase in Escherichia coli carrying hybrid ColE1 plasmids

3. Association of ATP: Glutamine Synthetase Adenylyltransferase Activity with the PI Component of the Glutamine Synthetase Deadenylylation System

4. Glutamine synthetase adenylyltransferase from Escherichia coli: purification and physical and chemical properties

5. Allosteric regulation of monocyclic interconvertible enzyme cascade systems: Use of Escherichia coli glutamine synthetase as an experimental model

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