| Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents |
1 | Autophosphorylat ion | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 0.001 (s^-1) | 0 (s^-1) | - | - | Substrate CheA
Product CheAp
|
| Autophosphorylation of CheA by ATP Kf = 0.001 /sec Kb = 0 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475 Reaction Scheme 1 |
2 | Autophosphorylat ion[1] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 0.0757 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate CheA TWA
Product CheAp
|
| TWA stimulated autophosphorylation of CheA TWA is complex of Tar, CheW and CheA Kf = 7.57*10e+04 /sec/M = 0.0757 /sec/uM As per Reaction 9 in 1REACT.BCT provided by Matthew Levin Kf = 5.9*10e+4 /sec/M = 0.059 /sec/uM Kb = 0 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475 Reaction Scheme 2 |
3 | Autophosphorylat ion[3] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 1 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate CheA TnWA
Product CheAp
|
| TnWA stimulated autophosphorylation of CheA TnWA is complex of Tar, CheW, CheA and Ni Kf = 1*10e+06 /sec/M = 1 /sec/uM Kb = 0 /sec As per Reaction 10 in 1REACT.BCT provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475, Reaction scheme 3 |
4 | Binding[2] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 4 (uM^-1 s^-1) | 10 (s^-1) | Kd(bf) = 2.5(uM) | - | Substrate CheA TW
Product TWA
|
| Binding of TW and CheA Kd = 0.3 uM and therefore Kf also suggested as 0.3 /sec/uM Kf = 4*10e5 /sec/M = 0.4 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 3 pp.476 Reaction Scheme 6 Rates used here are 10 times that stated, to allow for faster time courses seen during the drop of bias on removal of stimulus. |
5 | Binding[3] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 0.05 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 19.9999(uM) | - | Substrate CheA Tar
Product TA
|
| Binding of T and CheA Kf = 0.05 /sec/uM as per Reaction 3 in 1REACT.BCT Kf = 1*10e+04 /sec/M = 0.01 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 3 pp.476 Reaction Scheme 4 |
6 | Binding[4] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 0.05 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 19.9999(uM) | - | Substrate CheA Tn
Product TnA
|
| Binding of T-Ni and CheA Kf = 0.05 /sec/uM as per Reaction 3 in 1REACT.BCT Kf = 1*10e+04 /sec/M = 0.01 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 3 pp.476 Reaction Scheme 4 Footnote states that ligands do not have any effect on the formation of complexes so same rates are used for Aspartate or Ni associated Tar complexes. |
7 | Binding[5] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 4 (uM^-1 s^-1) | 10 (s^-1) | Kd(bf) = 2.5(uM) | - | Substrate CheA TnW
Product TnWA
|
| Binding of TnW and CheA Kf = 4*10e+05 /sec/M = 0.4 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 3 pp.476 Reaction Scheme 6 Footnote states that ligands do not have any effect on the formation of complexes so same rates are used for Aspartate or Ni associated tar complexes. |
8 | Binding[6] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 4 (uM^-1 s^-1) | 10 (s^-1) | Kd(bf) = 2.5(uM) | - | Substrate CheA TaW
Product TaWA
|
| Binding of TaW and CheA Kf = 4*10e+05 /sec/M = 0.4 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 3 pp.476 Reaction Scheme 6 Rates used here are 10 times that stated, to allow for faster time courses seen during the drop of bias on removal of stimulus. Footnote states that ligands do not have any effect on the formation of the Tar-CheW-CheA complex so same rates are used for Aspartate or Ni associated Tar complexes. |
9 | Binding[7] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 0.05 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 19.9999(uM) | - | Substrate CheA TA
Product TaA
|
| Binding of Tar-Aspartate and CheA Kf = 0.05 /sec/uM as per Reaction 3 in 1REACT.BCT Kf = 1e+04 /sec/M = 0.01 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 3 pp.476 Reaction Scheme 4 Footnote states that ligands do not have any effect on the formation of complexes so same rates are used for Aspartate or Ni associated Tar complexes. |
10 | Complexing[10] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 0.05 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 19.9999(uM) | - | Substrate CheA CheW
Product WA
|
| CheA and CheW complex formation Kf = 5*10e+04 /sec/M = 0.05 /sec/uM As per Reaction 4 in 1REACT.BCT provided by Matthew Levin Kf = 0.01 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 3 pp.476 Reaction Scheme 5 |