 |  |  GC |
|  |  Molecule |
| | Enzyme |
| | Reaction |
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Enzyme List for pathway GC (Pathway Number 177) | | Molecule Name/
Site Name | Km (uM) | kcat (1/s) | Ratio
(k2/k3) | Enzyme Type | Substrate | Product |
| 1 |
Enzyme Activity:
deph_NO2_sGC
Enzyme Molecule:
sGC-ppase* | 5 | 1.8 | 4 | explicit E-S complex | NO2.sGC_5coord
| deph_NO2.sGC
| | | similar to deph_NO_sGC.. |
| 2 |
Enzyme Activity:
deph_NO_sGC
Enzyme Molecule:
sGC-ppase* | 5 | 1.8 | 4 | explicit E-S complex | NO.sGC_5coord
| deph_NO.sGC
| | | Km and Vmax used from Ferrero et al., J Neurochem, 2000, 75: 2029-2039, and other refs cited in their paper. Though there are no plots in this paper, the rates look ok when the model is being run. Still this part can be improved further based on more experimental observations, since at the moment, there is not much information on the rates and kinetic details of the phosphatase mediated sGC regulation. |
| 3 |
Enzyme Activity:
sGC_act
Enzyme Molecule:
sGCtot | 30 | 22.05 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | GTP
| cGMP
| | | The range of estimates found in the literature are: Km -> 40 - 150 uM (without NO) 20 - 40 uM (with NO) Vmax -> 10 - 100 nmol/mg/min (wihtout NO) 10 - 40 umol/mg/min (with NO). ----- thru personal correspondence from T. Bellamy, Wolfson Ins. for Biomedical Sciences, UK. NO increases the Vmax of sGC by 100-200 fold, and it has been proposed that this activation occurs subsequent to the binding of NO toa heme moiety on the enzyme. (Stone and Marletta,1995, Biochemistry,34:14668-14674). |
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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