Identification of critical lysyl residues in the pyrophosphate-dependent phosphofructo-1-kinase of Propionibacterium freudenreichii
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00135a011
Reference8 articles.
1. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
2. Inactivation of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii by pyridoxal 5'-phosphate. Determination of the pH dependence of enzyme-reactant dissociation constants from protection against inactivation.
3. Spectroscopic Determination of Tryptophan and Tyrosine in Proteins*
4. Cloning, sequencing, and expression of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii.
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1. Influence of the Global Charge of the Protein on the Stability of Lysozyme–AuNP Bioconjugates;The Journal of Physical Chemistry C;2014-09-15
2. Effects of Chemical Modification of Lysine Residues on the Sweetness of Lysozyme;Chemical Senses;2005-03-01
3. Structure-Sweetness Relationship in Thaumatin: Importance of Lysine Residues;Chemical Senses;2001-02-01
4. The Pyrophosphate-Dependent Phosphofructokinase of the Protist, Trichomonas vaginalis, and the Evolutionary Relationships of Protist Phosphofructokinases;Journal of Molecular Evolution;1998-12
5. Involvement and identification of a lysine in the PPi-site of pyrophosphate-dependent phosphofructokinase from Giardia lamblia;Biochimie;1997-04
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