 |  |  GC |
|  |  Molecule |
| | Enzyme |
| | Reaction |
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Molecule List for pathway GC (Pathway Number 177) | | Name | Initial Conc. (uM) | Volume (fL) | Buffered | | 1 | deph_NO.sGC | 0 | 0.0016667 | No | | | | | 2 | deph_NO2.sGC | 0 | 0.0016667 | No | | | | | 3 | GTP | 10 | 0.0016667 | Yes | | | | | 4 | NO | 0.1 | 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.) | | 5 | NO.sGC6coord | 0 | 0.0016667 | No | | | this compoud, a 6-coordinate complex will be bound by another NO to an unidentified non-heme site in the next reaction step. | | 6 | NO.sGCfast | 0 | 0.0016667 | No | | | | | 7 | NO.sGCslow | 0 | 0.0016667 | No | | | | | 8 | NO.sGC_5coord | 0 | 0.0016667 | No | | | This is the active sGC, a 5-coordinate complex formed after a series of reaction steps, involving the formation of a 6 coordinate complex which converted to a 5-coordinate complex. | | 9 | NO.SGC_6coord | 0 | 0.0016667 | No | | | | | 10 | NO2.sGC_5coord | 0 | 0.0016667 | No | | | This is the 5-coordinate complex of the enzyme sGC. This is also the active form of the enzyme. | | 11 | nonhemebind_int | 0 | 0.0016667 | No | | | here the new NO has bound to the unidentified non-heme site on the 6-coordinate complex, and this will convert to the 5-coordinate complex. this binding of a new NO to the non-heme site on the 6-coordinate complex is characteristic of the slow binding process of NO to sGC. | | 12 | sGC-ppase | 0.5 | 0.0016667 | No | | | | | 13 | sGC-ppase* | 0 | 0.0016667 | No | | | | | 14 | sGCfast | 3 | 0.0016667 | Yes | | | 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 necessarily the 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) | | 15 | sGCslow | 3 | 0.0016667 | Yes | | | This is the slow reaction process of the binding of NO to sGC. we can notice the binding of another NO in the third reaction step to a non-heme site, which then converts to the 5-coordinate complex. this binding of another NO to an non-heme site is characteristic of the slow binding process of NO to sGC.(Stone and Marletta, 1996,35(4);1093-1099) 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.) | | 16 | sGCtot | 0 | 0.0016667 | No | | | This is the sumtotal of the sGC activated via two binding mecanisms as reported by Stone and Marletta, 1996, Biochemistry, 35(4):1093-1099. |
Summed Molecule List | | Target | Inputs | | 1 |
sGCtot | NO.sGC_5coord
NO2.sGC_5coord
| This is the sumtotal of the sGC activated via two binding mecanisms as reported by Stone and Marletta, 1996, Biochemistry, 35(4):1093-1099. |
Pathway Details Molecule List Enzyme List Reaction List
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