| | Name | Initial Conc. (uM) | Volume (fL) | Buffered |
| 1 | IP1(1) | 0 | 1000 | No |
| | Inositol (1)monophsophate Basal Conc ~ 44uM : Ackermann et al, BiochemJ 1987, 242(2): 517-24 IP metabolism maintains only a tenth of this level while the rest is generated from PtdIns metabolism. |
| 2 | IP1(3) | 0 | 1000 | No |
| | Inositol (3)monophosphate = 11% of Ins(1)P1 ~ 4.8uM Ackermann et al, Biochem J 242(2), 1987: 517 |
| 3 | ip1_1pase_cmplx | 0 | 1000 | No |
| | Enzyme complex exclusively modeled to accomodate enzyme reversibility as calculated from dG calculations for -5 kJ/mol. |
| 4 | IP2(13) | 0 | 1000 | No |
| | Inositol (13)bisphosphate |
| 5 | IP2(34) | 0 | 1000 | No |
| | Inositol (34)bisphosphate |
| 6 | IP2_3pase1 | 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 |
| 7 | IP2_3pase2 | 0.0094 | 1000 | No |
| | from Caldwell et al, JBC 266(27); 1991: 18378-86 enzyme is a heterodimer with one catalystic subunit and one regulatory 78 kDa subunit |
| 8 | IP_4pase | 0.9 | 1000 | No |
| | from Norris et al, JBC 269(12); 1994: 8716-20 Enzyme conc increased from 9 nM to 0.9 uM to obtain appreciable enzyme activity has two 4-phosphatase activities: against Ins(134)P3 and Ins(34)P2 respectively |
| 9 | IP_4pase_inact | 0 | 1000 | No |
| | |
