Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Energized submitochondrial particles were subjected to high or low [3H]ATP/[3H]ADP ratios, maintained during steady state by a pyruvate kinase or hexokinase regenerating system, respectively. Under both steady state conditions, about 1.4 mol [3H]nucleotide/mol ATPase was retained but considerably more [3H]ATP was retained with the high [3H]ATP/[3H]ADP ratio. The ATPase activity and the oxygen exchange of these differentially labeled SMP were the same, suggesting a lack of control function of non-catalytic tightly bound nucleotides.
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PMID:Catalytic properties of the ATPase on submitochondrial particles after exchange of tightly bound nucleotides under different steady state conditions. 622 36

This report delineates scope and limitation of the selectivity of synthetic multifunctional pores as enzyme sensors using glycolytic enzymes as example (G. Das, P. Talukdar, and S. Matile, Science, 2002, Vol. 298, pp. 1600-1602). Unproblematic detectability of hexokinase and phosphofructokinase demonstrates that the selectivity of synthetic multifunctional pore (SMPs) sensors suffices to sense ATP in mixed analytes containing ADP, whereas detection of the isomerization of glucose 6-phosphate into fructose 6-phosphate by phosphoglucose isomerase is not possible with confidence. The sensitivity of SMP sensors is sufficient for end-point detection of one picomole poly-L-glutamate hydrolyzed by papain in unoptimized assay format; the sensitivity of melittin as representative biological pore of similar charge and aggregation number to detect the same reaction is more than four orders of magnitude inferior.
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PMID:On selectivity and sensitivity of synthetic multifunctional pores as enzyme sensors: discrimination between ATP and ADP and comparison with biological pores. 1499 75