| | Name | Initial Conc. (uM) | Volume (fL) | Buffered |
| 1 | IP3(134) | 0 | 1000 | No |
| | Inositol (134)trisphosphate |
| 2 | IP3-56Kcmplx | 0 | 1000 | No |
| | enzyme substrate complex of IP3 56-K and Ins(134)P3. Complex exclusively modeled as reaction generates ratio of products, and because 5-kinase is reversible due to large Ins(1345)P4 backflux |
| 3 | IP3-56K_IP4-1K | 1.632 | 1000 | No |
| | Combined Ins(134)P3 5,6-kinase and Ins(3456)P4 1-kinase: from Yang and Shears, Biochem J 2000, 351: 551-555. Conc from Wilson and Majerus, JBC 271(20); 1996: 11904-10 5,6K Reaction products Ins(1346)P4 and Ins(1345)P4 are generated in a ratio of 2.3-5 : 1 Enzyme inhibition by products, as depicted in previous versions of the model, removed because it is now shown that enzyme is multi-tasking and reversible with respect to these products: Ho et al, Curr Biol 2002, 12: 1-20. This non M-M ability has been incorporated. But cycling to Ins(346)P3 by this enzyme not included because rest of Ins(346)P3 network biology is unknown in mammals. |
| 4 | IP4(1346) | 1 | 1000 | No |
| | Inositol (1346)tetrakisphosphate |
| 5 | IP4(1456) | 1 | 1000 | No |
| | Inositol(1456)tetrakisphosphate |
| 6 | IP4(3456) | 1.4 | 1000 | No |
| | Inositol (3456)tetrakisphosphate basal levels ~ 1.4uM |
| 7 | IP4-3K | 0.0048 | 1000 | No |
| | Ins(1456)P4 3kinase from Stephens et al, Biochem J 249; 1988: 283-92 |
| 8 | ip4_1k_cmplx | 0 | 1000 | No |
| | Enzyme complex exclusively modeled to accomodate reversible kinetics as opposed to M-M kinetics. Enzyme reversibility ascertained from dG calculations at -10 kJ/mol that yield a significant back flux from IP5. Also IP4-1K is experimentally reversible: Ho et al, Curr Biol, Mar 2002, 12: 1-20 |
| 9 | ip4_3k_cmplx | 0 | 1000 | No |
| | Enzyme complex exclusively modeled to include reversible kinetics, as the back flux is significant for dG = -10 kJ/mol |
| 10 | IP5(13456) | 53.9992 | 1000 | No |
| | Inositol(13456)pentakisphosphate Conc from Voglmaier et al, PNAS 93; 1996 |
