Spectrochemical evidence for the presence of a tyrosine residue in the allosteric site of glucosamine-6-phosphate deaminase from Escherichia coli
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1994.tb18638.x/fullpdf
Reference30 articles.
1. Sulfhydryl groups of glucosamine-6-phosphate isomerase deaminase from Escherichia coli
2. Evidence for vicinal thiols and their functional role in glucosamine-6-phosphate deaminase from Escherichia coli
3. Secondary structure of Escherichia coli glucosamine-6-phosphate deaminase from amino acid sequence and circular dichroism spectroscopy
4. Identification of two cysteine residues forming a pair of vicinal thiols in glucosamine-6-phosphate deaminase from Escherichia coli and a study of their functional role by site-directed mutagenesis
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2. Allosteric Activation of Escherichia coli Glucosamine-6-Phosphate Deaminase (NagB) In Vivo Justified by Intracellular Amino Sugar Metabolite Concentrations;Journal of Bacteriology;2016-06
3. The Tertiary Origin of the Allosteric Activation of E. coli Glucosamine-6-Phosphate Deaminase Studied by Sol-Gel Nanoencapsulation of Its T Conformer;PLoS ONE;2014-05-02
4. Why Does Escherichia coli Grow More Slowly on Glucosamine than on N -Acetylglucosamine? Effects of Enzyme Levels and Allosteric Activation of GlcN6P Deaminase (NagB) on Growth Rates;Journal of Bacteriology;2005-05
5. Structural flexibility, an essential component of the allosteric activation inEscherichia coliglucosamine-6-phosphate deaminase;Acta Crystallographica Section D Biological Crystallography;2001-12-21
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