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Molecule Parameter List for sGCfast | 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 |
| sGCfast 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 | 1 | 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 |
sGCfast acting as a Molecule in sGC_Stone_Marletta Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | sGCfast | sGC_Stone_
Marletta
Accession No. : 15 | sGC
Pathway No. : 69 | 3 | 0.0016667 | No | | Stone and Marletta, Biochemistry,35(4), 1996,. They have reported that the binding of sGC with NO occurs through two phases;a slow process and a fast process. 30% of the sGC binds quickly to NO; but the rest 70% goes through a slow process which involves the binding of another NO to an unidentified non-heme site on the protein, which seems to be not necessarilythe same site used in the initial two step binding to the heme. Stone and Marletta,1995,34;14668-14674;-- report that the native heme stoichiometry is 2 per heterodimer. spectrally only one type of heme is observed, indicating that both hemes are in similar environment. They conclude that each subunit of the heterodimer binds 1 equiv of heme at a site conserved between the two subunits. Concentration 3 uM assumed on the basis of reported data (Kuroda et al., J.Neurosci., 2001, 21(15): 5693-5702 ; Ariano et al., PNAS, 1982, 79:1316-1320) |
sGCfast 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 | | 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. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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