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Molecule Parameter List for cGMP | 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 | |
| Accession Name | Accession No. | Accession Type | Pathway Link | CO_activation_
of_GC | 28 | Pathway |
sGC | Carbon Monoxide is an activator of soluble Guanylyl Cyclase and has been implicated as a neuronal messenger [Ingi T. et al. Neuron (1996) 16(4):835-42].
CO binds to the heme group on sGC, similar to NO binding. Exogenous CO at similar conc. to endogenous levels were used to study the extent of activation of GC. Olfactory receptor neurons were used by Ingi et al., to investigate the relationship of CO to cGMP levels, as these cells have high levels of HO activity but no NOS activity.
Kharitonov VG. et al. Proc Natl Acad Sci U S A. (1995) 92(7):2568-71 and
Kharitonov VG. et al. Biochemistry (1999) 38(33):10699-706 report the presence of a six coordinate and a five coordinate intermediate of carboxy GC, induced by CO. Considering that activation of sGC by CO is similar in almost all tissues, some rates have been taken from original published works cited as references in Kharitonov et al., and Ingi et al., the primary datasources, this model is based on. |
cGMP acting as a Molecule in CO_activation_of_GC Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | cGMP | CO_activation_
of_GC
Accession No. : 28 | sGC
Pathway No. : 140 | 0 | 0.0016667 | No | | |
cGMP acting as a Substrate for an Enzyme in CO_activation_of_GC Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | PDE /
kenz | CO_activation_
of_GC
Accession No. : 28 | sGC
Pathway No. : 140 | 2 | 3.87 | 4 | explicit E-S complex | Substrate
cGMP
Product
5prime_GMP
| | Km / Vmax -- 2 uM / 3.87 sec^-1. rates from Turko et al., 1998, Biochem J, 329:505-510 and Kuroda et al., J Neurosci, 2001, 21(15):5693-5702 |
cGMP acting as a Product of an Enzyme in CO_activation_of_GC Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | GC5_CO /
activeGC | CO_activation_
of_GC
Accession No. : 28 | sGC
Pathway No. : 140 | 0.5 | 54.54 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | Substrate
GTP
Product
cGMP
| | Friebe et al., 1996, EMBO Journal, 15(24): 6863-6868 and back refs cited in their paper. They have studied the potentiation by YC-1 of CO activated sGC. In the absence of YC-1, they report 3 fold stimulation of GC by CO, with 218 +- 11 nmol/min/mg of cGMP. Vmax / Km increased by 100 X. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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