|
Enter a Search String | | Special character and space not allowed in the query term.
Search string should be at least 2 characters long. |
Molecule Parameter List for PP-IP5 | 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 | Osc_Ca_
IP3metabolism | 32 | Network |
MIPP, CaMKII, CaM,
PKC, IP3-3K, Gq,
PLCbeta, 134_dephos, 145_dephos,
IP4-system, IHP-system, 1345_dephos,
CaRegulation, Othmer-Tang-model | | This network models an oscillatory calcium response to GPCR mediated PLCbeta activation, alongwith detailed InsP3 metabolism in the neuron. It is similar to the Osc_Ca_IP3metab model (accession 24) except that some enzymes in the InsP3 metabolism network have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. The modified enzymes belong to the groups: IP4-system, IP3-3K, 145_dephos and 134_dephos. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. |
PP-IP5 acting as a Molecule in Osc_Ca_IP3metabolism Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | PP-IP5 | Osc_Ca_
IP3metabolism
Accession No. : 32 | IHP-system
Pathway No. : 168 | 2 | 1000 | No | | Diphosphoinositol pentakisphosphate Conc from Huang et al, Biochem 37; 1998 |
PP-IP5 acting as a Substrate for an Enzyme in Osc_Ca_IP3metabolism Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | DIPP1 /
dipp_ip7 | Osc_Ca_
IP3metabolism
Accession No. : 32 | IHP-system
Pathway No. : 168 | 0.340006 | 5.1 | 4 | explicit E-S complex | Substrate
PP-IP5
Product
IP6
| | from Safrany et al, EMBO J 17(22); 1998 Vmax represents activity of recombinant human protein which is 20-50 fold greater than activity of the purified rat enzyme |
PP-IP5 acting as a Product of an Enzyme in Osc_Ca_IP3metabolism Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | IP6_K2 /
ip6_k2 | Osc_Ca_
IP3metabolism
Accession No. : 32 | IHP-system
Pathway No. : 168 | 2.99999 | 1.633 | 4 | explicit E-S complex | Substrate
IP6
Product
PP-IP5
| | | from Saiardi et al, Curr Biol 9; 1999 | | 2 | DIPP1 /
dipp_ip8 | Osc_Ca_
IP3metabolism
Accession No. : 32 | IHP-system
Pathway No. : 168 | 0.0340035 | 0.6165 | 4 | explicit E-S complex | Substrate
bisPP-IP4
Product
PP-IP5
| | | from Safrany et al, EMBO J 17(22); 1998 Vmax represents activity of human recombinant protein, which is 20-50 fold greater than activity of the purified rat enzyme |
PP-IP5 acting as a Substrate in a reaction in Osc_Ca_IP3metabolism Network
| Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated.
Kd for higher order reaction are not consider. |
| Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | | PP-IP5cmplx-on | Osc_Ca_
IP3metabolism
Accession No. : 32 | IHP-system
Pathway No. : 168 | 0.0027
(uM^-2 s^-1) | 2.5
(s^-1) | - | - | Substrate
ATP
PP-IP5
PP-IP5-K
Product
PP-IP5-K-complex
| | from Huang et al, Biochem 37; 1998 Kf calculated using Km for PP-InsP5 and ATP, and Vmax of forward and backward reactions. Kb = Vmax of backward reaction |
PP-IP5 acting as a Product in a reaction in Osc_Ca_IP3metabolism Network
| Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated.
Kd for higher order reaction are not consider. |
| Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | | IP6cmplx-off | Osc_Ca_
IP3metabolism
Accession No. : 32 | IHP-system
Pathway No. : 168 | 1.26
(s^-1) | 0.0012
(uM^-2 s^-1) | - | - | Substrate
IP6-K-complex
Product
ADP
IP6-K
PP-IP5
| | from Voglmaier et al, PNAS 93; 1996 Kf = Vmax of forward reaction Kb calculated from Km for InsP6 and ATP, and Vmax of forward and backward reactions |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
|
