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- W2008291036 abstract "Results Recent studies have determined how ATP allosterically activates GC-A and GC-B [10]. In the absence of ATP, NPs activated these enzymes > 10-fold in a positive cooperative manner. In the absence of NP, ATP shifted the substrate-velocity profiles from cooperative to linear but did not change the Km. In the presence of NPs, ATP competed with GTP for binding to an allosteric site, which enhanced the activation of GCs by decreasing the Km. Thus, NP binding was required for communication of the allosteric activation signal to the catalytic site. Concentration-response assays determined that the ability of ATP to activate GCs decreased and enzyme potency increased with increasing GTP concentrations, consistent with reciprocal regulation of the allosteric and catalytic sites. Point mutations in the purine-binding site of the catalytic domain abolished GC activity but not allosteric activation. Co-expression of inactive mutants produced half the activity expected for symmetric catalytic dimers. 2’deoxy-ATP and 2’deoxy-GTP were poor allosteric activators, but 2’-deoxy-GTP was an effective substrate, consistent with distinct binding requirements for the allosteric and catalytic sites. Conclusion" @default.
- W2008291036 created "2016-06-24" @default.
- W2008291036 creator A5047095104 @default.
- W2008291036 date "2013-08-01" @default.
- W2008291036 modified "2023-10-06" @default.
- W2008291036 title "A twenty year journey to understand how ATP activates guanylyl cyclase A and B" @default.
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- W2008291036 doi "https://doi.org/10.1186/2050-6511-14-s1-o13" @default.
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