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Molecule Parameter List for GTP | 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 |
| GTP 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 | 0 | 0 | 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 |
GTP acting as a Molecule in sGC_Stone_Marletta Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | GTP | sGC_Stone_
Marletta
Accession No. : 15 | sGC
Pathway No. : 69 | 10 | 0.0016667 | No | | Concentration 10 uM (Kuroda et al., J.Neurosci., 2001, 21(15):5693-5702 ; Bhalla and Iyengar, 1999, Science, 283:381-387) |
GTP acting as a Substrate for an Enzyme in sGC_Stone_Marletta Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | sGCtot /
kenz | sGC_Stone_
Marletta
Accession No. : 15 | sGC
Pathway No. : 69 | 20 | 25.25 | 4 | explicit E-S complex | Substrate
GTP
Product
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). |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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