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Molecule Parameter List for Ta | The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network. The text color of a molecule is highlighted by color. | Statistics | Accession and Pathway Details | |
Accession Name | Accession No. | Accession Type | Pathway Link | Chemotaxis | 55 | Pathway | Chemotaxis | All parameters used are from the .BCT files for BCT1.1 provided by Matthew Levin from the Computational Biology Group in the Department of Zoology at the University of Cambridge.Bias does not reach 0.7, there is a lag in the response of bias to the 5 sec 1 uM Aspartate pulse as shown by Bray et al. Mol.Biol.Cell (1993) 4(5): 469-482. The June 2003 version of the BCT program is BCT4.3 and is available at the computational biology site of the Zoology department at Cambridge University. |
Ta acting as a Molecule in Chemotaxis Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | Ta | Chemotaxis Accession No. : 55 | Chemotaxis Pathway No. : 226 | 0 | 1.41 | No | Aspartate bound Tar Ta = 0.0 M As per Signal 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 | TA | Chemotaxis Accession No. : 55 | Chemotaxis Pathway No. : 226 | 1.55 | 1.41 | No | Tar-CheA complex TA = 1.55e-06 M = 1.55 uM As per Signal entry 9 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 |
Ta acting as a Substrate in a reaction in Chemotaxis Network
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 reaction are not consider. |
| Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | 1 | Complexing[2] | Chemotaxis Accession No. : 55 | Chemotaxis Pathway No. : 226 | 0.1 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 10.0003(uM) | - | Substrate CheW TA
Product 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. | 2 | Complexing[7] | Chemotaxis Accession No. : 55 | Chemotaxis Pathway No. : 226 | 0.4 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 2.5(uM) | - | Substrate CheW TA
Product 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 | 3 | Binding[7] | Chemotaxis Accession No. : 55 | Chemotaxis Pathway No. : 226 | 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. | 4 | Binding[11] | Chemotaxis Accession No. : 55 | Chemotaxis Pathway No. : 226 | 0.4 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 2.5(uM) | - | Substrate TA WA
Product 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. |
Ta acting as a Product in a reaction in Chemotaxis Network
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 reaction are not consider. |
| Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | 1 | Binding[1] | Chemotaxis Accession No. : 55 | Chemotaxis Pathway No. : 226 | 1.28 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 0.7813(uM) | - | Substrate Aspartate Tar
Product 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 | 2 | Binding[3] | Chemotaxis Accession No. : 55 | Chemotaxis Pathway No. : 226 | 0.05 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 19.9999(uM) | - | Substrate CheA Tar
Product 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 |
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