Involvement of arginine residues in the allosteric activation of Escherichia coli ADP-glucose synthetase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00537a036
Cited by 19 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Identification of Functionally Important Amino-Terminal Arginines of Agrobacterium tumefaciens ADP-Glucose Pyrophosphorylase by Alanine Scanning Mutagenesis;Biochemistry;2001-08-01
2. Characterization of ADP-Glucose Pyrophosphorylase from Rhodobacter sphaeroides 2.4.1: Evidence for the Involvement of Arginine in Allosteric Regulation;Archives of Biochemistry and Biophysics;1999-12
3. Arginine294 Is Essential for the Inhibition of Anabaena PCC 7120 ADP-Glucose Pyrophosphorylase by Phosphate;Biochemistry;1997-10-01
4. Evidence for essential arginine residues at the active sites of maize branching enzymes;Journal of Protein Chemistry;1996-04
5. Identification of amino acid residues involved in the activity of phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa.;Journal of Biological Chemistry;1994-02
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