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• W2004651510 abstract "The allosteric regulation of binding to and the activation of cGMP-dependent protein kinase (cGMP kinase) was studied under identical conditions at 30°C using three forms of cGMP-kinase which differed in the aminoterminal segment, e.g. native cGMP kinase, phosphorylated cGMP kinase which contained 1.4±0.4 mol phosphate/subunit and constitutively active cGMP kinase which lacked the amino-terminal dimerization domain. These three enzyme forms have identical kinetic constants, e.g. number of cGMP-binding sites, Km values for MgATP and the heptapeptide Kemptide, and Vmax values. In the native enzyme, MgATP decreases the affinity for binding site 1. This effect is abolished by 1 M NaCl. In contrast, high concentrtions of Kemptide increase the affinity of binding site 2 about fivefold. Under the latter conditions, identical Kd values of 0.2 μM were obtained for sites 1 and 2. Salt, MgATP and Kemptide do not affect the binding kinetics of the phosphorylated or the constitutively active enzyme, suggesting that allosteric regulation depends solely on the presence of a native amino-terminal segment. Cyclic GMP activates the native enzyme at Ka values which are identical with the Kd values for both binding sites. The activation of cGMP-dependent protein kinase is noncooperative but the Ka value depends on the substrate peptide concentration. These results show that the activity of cGMP kinase is primarily regulated by conformational changes within the amino-terminal domain." @default.
• W2004651510 created "2016-06-24" @default.
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• W2004651510 creator A5091874127 @default.
• W2004651510 date "1989-05-01" @default.
• W2004651510 modified "2023-10-14" @default.
• W2004651510 title "The amino terminus regulates binding to and activation of cGMP-dependent protein kinase" @default.
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• W2004651510 doi "https://doi.org/10.1111/j.1432-1033.1989.tb14771.x" @default.
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