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Reaction List for pathway Chemotaxis (Pathway Number 226) |
| Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated. Kd for higher order reactions is not considered. |
| Name | Kf | Kb | Kd | tau | Substrate | Product | |
| 1 | Autodephosphoryl ation | 1 (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] | 0.037 (s^-1) | 0 (s^-1) | - | - | CheYp | CheY |
| Tar-CheW complex TW = 1.88e-06 M = 1.88 uM As per Signal entry 3 in 1SIG_B.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 3 | Autophosphorylat ion | 0.001 (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] | 0.0757 (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] | 0 () | 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] | 1 (uM^-1 s^-1) | 0 (s^-1) | - | - | TnWA CheA | CheAp |
| Aspartate bound Tar and CheW complex TaW = 0 M As per Signal 7 in 1SIG_B.BCT Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 7 | Binding | 0.001 (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] | 0.4 (uM^-1 s^-1) | 1 (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 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] | 0.4 (uM^-1 s^-1) | 1 (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 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] | 1.28 (uM^-1 s^-1) | 1 (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] | 0.4 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 2.5(uM) | - | TW CheA | TWA |
| MYpYpYpYp = 1.51e-09 M = 1.51e-3 uM As per Signal 27 in 1SIG_B.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 12 | Binding[3] | 0.05 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 19.9999(uM) | - | Tar CheA | TA |
| Tar-Asp-CheA complex TaA = 0 M As per Signal 10 in 1SIG_B.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 13 | Binding[4] | 0.05 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 19.9999(uM) | - | Tn CheA | TnA |
| Bias calculated as per formula stated on pp.471 Bias = [M + MYp] / [M + MYp + MYpYp + MYpYpYp + MYpYpYpYp] Bray et al 1993, Mol.Biol.Cell 4: 469-482 Initialy set to 0.7 | |||||||
| 14 | Binding[5] | 0.4 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 2.5(uM) | - | TnW CheA | TnWA |
| MYp = 9.53*e-10 M = 9.53*e-4 uM As per Signal 24 in 1SIG_B.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 15 | Binding[6] | 0.4 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 2.5(uM) | - | TaW CheA | TaWA |
| Motor = 8.5 molecules per cell As per Enzyme entry 7 in 1ENZ.BCT provided by Matthew Levin Motor = 6.73e-9 M = 6.73e-3 uM As per Signal 23 in 1SIG_B.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 16 | Binding[7] | 0.05 (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] | 0.4 (uM^-1 s^-1) | 1 (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 | |||||||
| 18 | Complexing | 0.1 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 10.0003(uM) | - | CheW Tar | TW |
| CheYp = 1.24e-07 M = 1.24e-01 uM As per Signal 22 in 1SIG_B.BCT provided by Matthew Levin CheYp = 1e-08 M = 1e-2 uM As per Set_Yp configuration in 1CONFIG.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 19 | Complexing[10] | 0.05 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 19.9999(uM) | - | CheW CheA | WA |
| 20 | Complexing[1] | 0.1 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 10.0003(uM) | - | Tn CheW | TnW |
| Nickel bound Tar and CheW complex TnW = 0.0 uM As per Signal 8 in 1SIG_B.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 21 | Complexing[2] | 0.1 (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] | 88.0009 (uM^-1 s^-1) | 5.5 (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] | 285 (uM^-1 s^-1) | 6.64 (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] | 693.999 (uM^-1 s^-1) | 5.1 (s^-1) | Kd(bf) = 0.0073(uM) | - | CheYp MYpYp | MYpYpYp |
| Tar-Ni-CheW-CheA complex TnWA = 0 M As per Signal 15 in 1SIG.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 25 | Complexing[6] | 2006.97 (uM^-1 s^-1) | 5.5 (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] | 0.4 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 2.5(uM) | - | TA CheW | TWA |
| Denominator value to calculate bias as stated on pp.471 Bias = [M + MYp] / [M + MYp + MYpYp + MYpYpYp + MYpYpYpYp] Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 27 | Complexing[8] | 0.4 (uM^-1 s^-1) | 1 (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 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] | 0.4 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 2.5(uM) | - | TaA CheW | TaWA |
| 29 | Dephosphorylatio n | 0.5 (uM^-1 s^-1) | 0 (s^-1) | - | - | CheYp CheZ | CheY |
| Ni bound Tar Ni-Tar = 0 M As per Signal 4 in 1SIG_B.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 30 | Dephosphorylatio n[1] | 99.9972 (uM^-1 s^-1) | 0 (s^-1) | - | - | CheYp TaWA | CheY |
| MYpYpYp = 4.47e-10 M = 4.47e-4 uM As per Signal 26 in 1SIG_B.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482 | |||||||
| 31 | Phosphotransfer | 1 (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] | 0.27 (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 | |||||||
| Pathway Detail | Molecule List | Enzyme List | Reaction List |