Literature DB >> 6124275

Escherichia coli glutamine synthetase. Determination of rate-limiting steps by rapid-quench and isotope partitioning experiments.

T D Meek, K A Johnson, J J Villafranca.   

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Year:  1982        PMID: 6124275     DOI: 10.1021/bi00538a027

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


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  5 in total

1.  Probing fast ribozyme reactions under biological conditions with rapid quench-flow kinetics.

Authors:  Jamie L Bingaman; Kyle J Messina; Philip C Bevilacqua
Journal:  Methods       Date:  2017-03-14       Impact factor: 3.608

2.  Mechanistic Basis for ATP-Dependent Inhibition of Glutamine Synthetase by Tabtoxinine-β-lactam.

Authors:  Garrett J Patrick; Luting Fang; Jacob Schaefer; Sukrit Singh; Gregory R Bowman; Timothy A Wencewicz
Journal:  Biochemistry       Date:  2017-10-31       Impact factor: 3.162

3.  Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated pup intermediate.

Authors:  Ethan Guth; Michael Thommen; Eilika Weber-Ban
Journal:  J Biol Chem       Date:  2010-11-16       Impact factor: 5.157

4.  Investigating the effects of posttranslational adenylylation on the metal binding sites of Escherichia coli glutamine synthetase using lanthanide luminescence spectroscopy.

Authors:  L P Reynaldo; J J Villafranca; W D Horrocks
Journal:  Protein Sci       Date:  1996-12       Impact factor: 6.725

5.  Time-resolved fluorescence studies of tryptophan mutants of Escherichia coli glutamine synthetase: conformational analysis of intermediates and transition-state complexes.

Authors:  W M Atkins; J J Villafranca
Journal:  Protein Sci       Date:  1992-03       Impact factor: 6.725

  5 in total

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