Kinetic studies and properties of potato apyrase
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Cited by (69)
Screening of plant derived chalcones on the inhibition of potato apyrase: Potential protein biotechnological applications in health
2020, International Journal of Biological MacromoleculesCitation Excerpt :As shown by our results, sera of immunized mice were able to recognize a protein band of 50 kDa at all dilutions used. This weight corroborates with the predicted mass range for S. tuberosum apyrase according to previous studies [2,4,6,30,31]. In addition, the phosphohydrolytic activity was evaluated in a non-denaturing gel, and the ATPase and ADPase activity of the purified protein was confirmed by deposition of calcium phosphate for the two nucleotides used, ATP and ADP (data not shown).
Efficient Catalysis of Protein Folding by GroEL/ES of the Obligate Chaperonin Substrate MetF
2020, Journal of Molecular BiologyAnalysis of read length limiting factors in Pyrosequencing chemistry
2007, Analytical BiochemistryCitation Excerpt :The first is to enhance enzymatic nucleotide removal efficiency in degrading excess nucleotides. The apyrase used in the four-enzyme Pyrosequencing system is obtained from Solanum tubersom, which demonstrates 90% higher efficiency in degrading dNTP to dNDP than in degrading dNDP to dNMP [28] Thus, the main product inhibition of apyrase is due to accumulation of dNDP, rather than dNMP, in the solution. Adding a small amount of dNDP- and dNMP-degrading enzymes would potentially increase the efficiency of nucleotide degradation, thereby allowing longer reads.
Folding of CFTR is predominantly cotranslational
2005, Molecular CellCitation Excerpt :We found that ATP depletion by apyrase had a drastic effect on CFTR structure, whereas ATP depletion by hexokinase and glucose did not. Apyrase can convert ATP all the way down to inorganic phosphate (Taussky and Shorr, 1953; Traverso-Cori et al., 1965), whereas hexokinase converts ATP to ADP. CFTR structure and function is likely to be affected directly because NBD domains bind ATP or ADP (Aleksandrov et al., 2001; Vergani et al., 2005).
Fluorescent ε-ATP analogues for probing physicochemical properties of proteins. Synthesis, biochemical evaluation, and sensitivity to properties of the medium
2004, Bioorganic and Medicinal ChemistryCitation Excerpt :Only limited information is available on the properties of NTPDases binding site. Few chemical modifications32 or site-directed mutagenesis studies showed important amino acids and a sequence corresponding to phosphate binding motifs.33 The physicochemical characteristics of the NTPDase binding site are still unknown.
A mathematical model of the Pyrosequencing reaction system
2004, Biophysical Chemistry