| | Name | Kf | Kb | Kd | tau | Substrate | Product |
| 1 |
Autodephosphoryl
ation | kf
(s^-1) | 0
(s^-1) | - | - | CheBp
| CheB
|
| | Autodephosphorylation of CheBp Kf = 1 /sec Kb = 0 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475 Reaction Scheme 10 |
| 2 |
Autodephosphoryl
ation[1] | kf
(s^-1) | 0
(s^-1) | - | - | CheYp
| CheY
|
| | Autodephosphorylation of CheYp Kf = 3.7*10e-02 /sec Kb = 0 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475 Reaction Scheme 7 |
| 3 |
Autophosphorylat
ion | kf
(s^-1) | 0
(s^-1) | - | - | CheA
| 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 |
| 4 |
Autophosphorylat
ion[1] | kf
(uM^-1 s^-1) | 0
(s^-1) | - | - | TWA
CheA
| 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 |
| 5 |
Autophosphorylat
ion[2] | kf
() | 0
(s^-1) | - | - | - | CheYp
|
| | Autophosphorylation of CheY Paper says reaction not applicable Table 2 pp.475 Reaction Scheme 6 kf = 0/sec kb = 0/sec As per Reaction 14 in 1REACT.BCT provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482 |
| 6 |
Autophosphorylat
ion[3] | kf
(uM^-1 s^-1) | 0
(s^-1) | - | - | TnWA
CheA
| 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 |
| 7 |
Binding | kf
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 1000.028(uM) | - | Ni
Tar
| Tn
|
| | Binding of Tar and Ni Kf = 1 * 10e+03 /sec/M = 0.001 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 3 pp.476 Reaction Scheme 2 |
| 8 |
Binding[10] | kf
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 2.5(uM) | - | Tn
WA
| TnWA
|
| | Binding of Tn and CheW-CheA complex Kf = 4e+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 8 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 complexes so same rates are used for Aspartate or Ni associated Tar complexes. |
| 9 |
Binding[11] | kf
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 2.5(uM) | - | TA
WA
| TaWA
|
| | Binding of Ta and CheW-CheA complex Kf = 4e+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 8 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 the formation of complexes so same rates are used for Aspartate or Ni associated Tar complexes. |
| 10 |
Binding[1] | kf
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 0.7813(uM) | - | Aspartate
Tar
| TA
|
| | Binding of Aspartate with Tar Kd = 0.78 uM Dunten and Koshland, 1991 Kf = 1.28e+06 /sec/M = 1.28 /sec/uM here scaled by 5 As per Reaction 0 in 1REACT.BCT provided by Matthew Levin Kf = 1.0e+06 /sec/M = 1 /sec/uM; Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 3 pp.476 Reaction Scheme 1 |
| 11 |
Binding[2] | kf
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 2.5(uM) | - | TW
CheA
| 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. |
| 12 |
Binding[3] | kf
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 19.9999(uM) | - | Tar
CheA
| 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 |
| 13 |
Binding[4] | kf
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 19.9999(uM) | - | Tn
CheA
| 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. |
| 14 |
Binding[5] | kf
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 2.5(uM) | - | TnW
CheA
| 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. |
| 15 |
Binding[6] | kf
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 2.5(uM) | - | TaW
CheA
| 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. |
| 16 |
Binding[7] | kf
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 19.9999(uM) | - | TA
CheA
| 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. |
| 17 |
Binding[9] | kf
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 2.5(uM) | - | WA
Tar
| TWA
|
| | Binding of Tar and CheW-CheA complex Kd = 2 uM and therefore Kf also suggested as 0.5 /sec/uM Kf = 4e+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 8 Rates used here are 10 times that stated, to allow for faster time courses seen during the drop of bias on removal of stimulus. |
| 18 |
Complexing | kf
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 10.0003(uM) | - | CheW
Tar
| TW
|
| | Tar and CheW complex formation Kf = 1 * 10e5 /sec/M = 0.1 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 3 pp.476 Reaction Scheme 3 |
| 19 |
Complexing[10] | kf
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 19.9999(uM) | - | CheW
CheA
| 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 |
| 20 |
Complexing[1] | kf
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 10.0003(uM) | - | Tn
CheW
| TnW
|
| | Complex formation of Ni bound Tar and CheW Kf = 1 * 10e5 /sec/M = 0.1 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482; Table 3 pp.476 Reaction Scheme 3 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. |
| 21 |
Complexing[2] | kf
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 10.0003(uM) | - | TA
CheW
| TaW
|
| | Complex formation of aspartate bound Tar and CheW Kf = 1 * 10e+05 /sec/M = 0.1 /sec/uM Kb = 1 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482; Table 3 pp.476 Reaction Scheme 3 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. |
| 22 |
Complexing[3] | kf
(uM^-1 s^-1) | 55
(s^-1) | Kd(bf) = 0.0625(uM) | - | CheYp
Motor
| MYp
|
| | CheYp complexes with Flagellar Motor (M) Kf = 0.88/Set_Yp = 0.88/1e-08 /sec/M = 0.88e+2/sec/uM Kb = 5.5 /sec As per EXEC.C provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482 |
| 23 |
Complexing[4] | kf
(uM^-1 s^-1) | 66.4
(s^-1) | Kd(bf) = 0.0233(uM) | - | CheYp
MYp
| MYpYp
|
| | CheYp complexes with MYp Kf = 2.85/Set_Yp = 2.85/1e-08 /sec/M = 2.85e+2/sec/uM Kb = 6.64 /sec As per EXEC.C provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482 |
| 24 |
Complexing[5] | kf
(uM^-1 s^-1) | 51
(s^-1) | Kd(bf) = 0.0073(uM) | - | CheYp
MYpYp
| MYpYpYp
|
| | CheYp complexes with MYpYp Kf = 6.94/Set_Yp = 6.94/1e-08 /sec/M = 6.94e+2 /sec/uM Kb = 5.1 /sec As per EXEC.C provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482 |
| 25 |
Complexing[6] | kf
(uM^-1 s^-1) | 55
(s^-1) | Kd(bf) = 0.0027(uM) | - | CheYp
MYpYpYp
| MYpYpYpYp
|
| | CheYp complexes with MYpYpYp Kf = 20.07/Set_Yp = 20.07/1e-08 /sec/M = 20.07e+2 /sec/uM Kb = 5.5 /sec As per EXEC.C provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482 |
| 26 |
Complexing[7] | kf
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 2.5(uM) | - | TA
CheW
| TWA
|
| | TA and CheW complex formation Kf = 4*10e+05 /sec/M = 0.4 /sec/uM Kb = 1 /sec Table 3 pp.476 Reaction Scheme 7 Bray et al 1993, Mol.Biol.Cell 4: 469-482 Rates used here are 10 times that stated, to allow for faster time courses seen during the drop of bias on removal of stimulus. |
| 27 |
Complexing[8] | kf
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 2.5(uM) | - | TnA
CheW
| TnWA
|
| | TnA and CheW complex formation 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 7 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 Tar-CheW-CheA complex so same rates are used for Aspartate or Ni associated Tar complexes. |
| 28 |
Complexing[9] | kf
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 2.5(uM) | - | TaA
CheW
| TaWA
|
| | TaA and CheW complex formation 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 7 Rates used here are 10 time 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 |
| 29 |
Dephosphorylatio
n | kf
(uM^-1 s^-1) | 0
(s^-1) | - | - | CheYp
CheZ
| CheY
|
| | CheZ stimulated dephosphorylation of CheYp Kf = 5*10e+05 /sec/M = 0.5 /sec/uM Kb = 0 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475 Reaction Scheme 8 |
| 30 |
Dephosphorylatio
n[1] | kf
(uM^-1 s^-1) | 0
(s^-1) | - | - | CheYp
TaWA
| CheY
|
| | TWA-aspartate stimulated dephosphorylation of CheYp Kf = 1 * 10e08 /sec/M = 100 /sec/uM Kb = 0 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475 Reaction Scheme 4 |
| 31 |
Phosphotransfer | kf
(uM^-1 s^-1) | 0
(uM^-1 s^-1) | - | - | CheAp
CheB
| CheBp
CheA
|
| | Phosphotransfer from CheAp to CheB Kf = 1 * 10e6 /sec/M = 1 /sec/uM Kb = 0 /sec/M Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475 Reaction Scheme 9 |
| 32 |
Phosphotransfer[
1] | kf
(uM^-1 s^-1) | 0
(uM^-1 s^-1) | - | - | CheAp
CheY
| CheYp
CheA
|
| | Phosphotransfer from CheAp to CheY Kf = 2 * 10e+05 /sec/M = 0.2 /sec/uM Kb = 0 /sec/M Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475 Reaction Scheme 5 |
