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Modelling the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase on adenylate kinase
Journal Article Research Support, Non-U.S. Gov't --- Old month value: Feb 1
Simultaneous multiple alignment of available sequences of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase revealed several segments of conserved residues in the 2-kinase domain. The sequence of the kinase domain was also compared with proteins of known three-dimensional structure. No similarity was found between the kinase domain of 6-phosphofructo-2-kinase and 6-phosphofructo-1-kinase. This questions the modelling of the 2-kinase domain on bacterial 6-phosphofructo-1-kinase that has previously been proposed [Bazan, Fletterick and Pilkis (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 9642-9646]. However, sequence similarities were found between the 2-kinase domain and several nucleotide-binding proteins, the most similar being adenylate kinase. A structural model of the 2-kinase domain based on adenylate kinase is proposed. It accommodates all the results of site-directed mutagenesis studies carried out to date on residues in the 2-kinase domain. It also allows residues potentially involved in catalysis and/or substrate binding to be predicted.
Adenylate Kinase/*chemistry Amino Acid Sequence Animals Escherichia coli/enzymology Fructose-Bisphosphatase/*chemistry/metabolism Fungal Proteins/chemistry Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed/genetics Phosphofructokinase-1/*chemistry/metabolism Phosphofructokinase-2 Phosphotransferases (Alcohol Group Acceptor)/*chemistry/metabolism Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment
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