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Molecule Parameter List for NO | 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 |
| NO participated as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction | | No. of occurrences | 1 | 0 | 0 | 0 | 0 | 3 | 0 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | sGC_Stone_
Marletta | 15 | Pathway |
sGC | | This features the two step binding of NO to soluble Guanylyl Cyclase as proposed by Stone JR, Marletta MA. Biochemistry (1996) 35(4):1093-9. There is a fast step binding scheme and a slow step binding scheme. The difference lies in the binding of a NO to a non-heme site on sGC, which may not necessarily be the same site of binding during the initial binding. The rates have been directly used from their models |
NO acting as a Molecule in sGC_Stone_Marletta Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | NO | sGC_Stone_
Marletta
Accession No. : 15 | sGC
Pathway No. : 69 | 0 | 0.0016667 | No | | Endogenously produced NO concentrations in the course of signal transduction processes are < 100 nM. (Varner et al., Nitric oxide in the nervous system, Academic press, London, UK, pp.191-206.) |
NO acting as a Substrate in a reaction in sGC_Stone_Marletta 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 | NO_bind_sGCfast | sGC_Stone_
Marletta
Accession No. : 15 | sGC
Pathway No. : 69 | 700
(uM^-1 s^-1) | 800
(s^-1) | Kd(bf) = 1.1429(uM) | - | Substrate
NO
sGCfast
Product
NO.sGCfast
| | | This is the fast binding of NO to sGC, subsequently activating it, as proposed by Stone and Marletta. Rates of these binding reactions used directly from Stone and Marletta,1996, Biochemistry, 35(4):1093-1099, based on whose paper this model is made. Rates obtained from stopped flow kinetics detailed in their paper. | | 2 | NObindnonheme | sGC_Stone_
Marletta
Accession No. : 15 | sGC
Pathway No. : 69 | 5
(uM^-1 s^-1) | 25
(s^-1) | Kd(bf) = 5(uM) | - | Substrate
NO
NO.sGC6coord
Product
nonhemebind_int
| | | This step is the one that differs from the fast reaction scheme, as reported by Stone and Marletta. Here the reaction is dependent upon the binding of NO to an unidentified non-heme site on the protein. Rates used directly from Stone and Marletta,1996, Biochemistry, 35(4):1093-1099. | | 3 | NO_bind_sGCslow | sGC_Stone_
Marletta
Accession No. : 15 | sGC
Pathway No. : 69 | 700
(uM^-1 s^-1) | 800
(s^-1) | Kd(bf) = 1.1429(uM) | - | Substrate
NO
sGCslow
Product
NO.sGCslow
| | | This is the slow binding of NO to sGC, as reported by Stone and Marletta,1996, Biochemistry, 35(4):1093-1099.The rates shown have been used directly from their data from stopped flow kinetics. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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