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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 asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1001000

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • sGC_Stone_
    Marletta
  • 15Pathway
    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
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    GTP
  • sGC_Stone_
    Marletta

    Accession No. : 15
  • sGC
    Pathway No. : 69
    100.0016667No
    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 NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    sGCtot  /
    kenz
  • sGC_Stone_
    Marletta

    Accession No. : 15
  • sGC
    Pathway No. : 69
    2025.254explicit E-S complexSubstrate
    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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