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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

cGMP 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	1	1	0	0

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.