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Molecule Parameter List for cAMP | The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network.
The text color of a molecule is highlighted by  color. | | Statistics |
Accession and Pathway Details | |
cAMP acting as a Molecule in cAMP_pathway Network
cAMP acting as a Substrate for an Enzyme in cAMP_pathway Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | cAMP-PDE /
PDE | cAMP_pathway
Accession No. : 25 | AC
Pathway No. : 136 | 19.8413 | 10 | 4 | explicit E-S complex | Substrate
cAMP
Product
AMP
| | | Best rates are from Conti et al Biochem 34 7979-7987 1995. Though these are for the Sertoli cell form, it looks like they carry nicely into alternatively spliced brain form. See Sette et al JBC 269:28 18271-18274 Km ~2 uM, Vmax est ~ 10 umol/min/mg for pure form. Brain protein is 93 kD but this was 67. So k3 ~10, k2 ~40, k1 ~4.2e-6 | | 2 | cAMP-PDE* /
PDE* | cAMP_pathway
Accession No. : 25 | AC
Pathway No. : 136 | 19.8413 | 20 | 4 | explicit E-S complex | Substrate
cAMP
Product
AMP
| | | This form has about twice the activity of the unphosphorylated form. See Sette et al JBC 269:28 18271-18274 1994. We'll ignore cGMP effects for now. |
cAMP acting as a Product of an Enzyme in cAMP_pathway Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | Gs.AC /
cyclase | cAMP_pathway
Accession No. : 25 | AC
Pathway No. : 136 | 20 | 18 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | Substrate
ATP
Product
cAMP
| | See Feinstein et al PNAS 88:10173-10177, Jacobowitz et al JBC 286(6):3829-3832 Smigel, JBC 261(4):1976-1982 (1986) |
cAMP acting as a Substrate in a reaction in cAMP_pathway Network
| 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 reaction are not consider. |
| | Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | | 1 | cAMP-bind-site-B
1 | cAMP_pathway
Accession No. : 25 | PKA
Pathway No. : 135 | 54
(uM^-1 s^-1) | 33
(s^-1) | Kd(bf) = 0.6111(uM) | - | Substrate
R2C2
cAMP
Product
cAMP.R2C2
| | | Hasler et al FASEB J 6:2734-2741 1992 say Kd =1e-7M for type II, 5.6e-8 M for type I. Take mean which comes to 2e-13 #/cell Smith et al PNAS USA 78:3 1591-1595 1981 have better data. First kf/kb=2.1e7/M = 3.5e-5 (#/cell). Ogreid and Doskeland Febs Lett 129:2 287-292 1981 have figs suggesting time course of complete assoc is < 1 min. | | 2 | cAMP-bind-site-B
2 | cAMP_pathway
Accession No. : 25 | PKA
Pathway No. : 135 | 54
(uM^-1 s^-1) | 33
(s^-1) | Kd(bf) = 0.6111(uM) | - | Substrate
cAMP
cAMP.R2C2
Product
cAMP2.R2C2
| | | For now let us set this to the same Km (1e-7M) as site B. This gives kf/kb = .7e-7M * 1e6 / (6e5^2) : 1/(6e5^2) = 2e-13:2.77e-12 Smith et al have better values. They say that this is cooperative, so the consts are now kf/kb =8.3e-4 | | 3 | cAMP-bind-site-A
1 | cAMP_pathway
Accession No. : 25 | PKA
Pathway No. : 135 | 75
(uM^-1 s^-1) | 110
(s^-1) | Kd(bf) = 1.4667(uM) | - | Substrate
cAMP
cAMP2.R2C2
Product
cAMP3.R2C2
| | 4 | cAMP-bind-site-A
2 | cAMP_pathway
Accession No. : 25 | PKA
Pathway No. : 135 | 75
(uM^-1 s^-1) | 32.5
(s^-1) | Kd(bf) = 0.4333(uM) | - | Substrate
cAMP
cAMP3.R2C2
Product
cAMP4.R2C2
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| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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