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Reaction List for pathway PDE (Pathway Number 178) | | Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated. Kd for higher order reactions is not considered. |
| | Name | Kf | Kb | Kd | tau | Substrate | Product | | 1 |
cGMPbindcGK | kf
(uM^-1 s^-1) | 81
(s^-1) | Kd(bf) = 8.1(uM) | - | cGMP
cGK
| cGMP.PKG
| | | Kinase activation in both the isoforms of cGK depends on cyclic nucleotide occupation of the two cyclic nucleotide binding sites in the regulatory domain. This event is supposed to reduce the affinity of the auto-inhibition region of the regulatory domain for the catalytic domain. Investigations revealed that cGMP binds to a slowly dissociating cyclic nucleotide binding site and induces a conformational change resulting in a partially active kinase. Subsequent occupation of the second, rapid dissociation site imparts additional conformational change until it forms the elongated shape that is reported to be associated with the fully active enzyme. (Taylor et al., 2000, JBC, 275(36):28053-28062) Dissociation rates for cGKII binding sites from Taylor et al., 2000, and other refs cited in their paper. cGMP dissociation from slow site -- 8.1/s (Smith et al., JBC,1995, 271(34):20756-20762) | | 2 |
fast_site_bind | kf
(uM^-1 s^-1) | 37
(s^-1) | Kd(bf) = 3.7(uM) | - | cGMP.PKG
cGMP
| cGMP2.PKG
| | 3 |
PDEbind_cGMP | kf
(uM^-1 s^-1) | 13
(s^-1) | Kd(bf) = 1.3(uM) | - | cGMP
PDE
| cGMP.PDE
| | | Kd ~1.3 uM. (Turko et al., JBC, 1996, 271(36):22240-22244, and Corbin et al., Eur J Biochem, 2000,267:2760-2767) |
Pathway Details Molecule List Enzyme List Reaction List
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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