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Molecule Parameter List for IP2_3pase1 | 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 |
IP2_3pase1 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 | 1 | 0 | 0 | 0 | 0 |
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. |
IP2_3pase1 acting as a Molecule in Osc_Ca_IP3metabolism Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | IP2_3pase1 | Osc_Ca_ IP3metabolism Accession No. : 32 | 134_dephos Pathway No. : 165 | 0.0038 | 1000 | No | from Caldwell et al, JBC 266(27); 1991: 18378-86 Enzyme is a homodimer with two catalytic subunits. Conc of enzyme increased 2 times from 1.9 nM to account for two monomeric subunit pools |
IP2_3pase1 acting as an Enzyme in Osc_Ca_IP3metabolism Network
Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | IP2_3pase1 / ip2_3pase1
| Osc_Ca_ IP3metabolism Accession No. : 32 | 134_dephos Pathway No. : 165 | 0.799992 | 117.33 | 4 | explicit E-S complex | Substrate IP2(13)
Product IP1(1)
| from Caldwell et al, JBC 266; 1991 enzyme activity was assayed for the monomeric form of the enzyme |
| 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. |
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