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Molecule Parameter List for TaWA | 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 | 57 | Pathway | Chemotaxis | Reactions feeding into TnWa, TaWA and TWA are scaled by 10 Binding reaction of Tar with Aspartate has been scaled by 10 Phosphotransfer from CheAp to CheY has Kb = 0.263/sec/uM instead of 0.2/sec/uM used in BCT1.1. All remaining parameters 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. 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. Citation: Bray et al. Mol.Biol.Cell (1993) 4(5): 469-482. |
TaWA acting as a Molecule in Chemotaxis Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | TaWA | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 0 | 1.41 | No | Tar-CheW-CheA-Aspartate complex TaWA = 0 M As per Signal 14 in 1SIG_B.BCT provided by Matthew Levin Cell volume = 1.41e-15 L Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 1. pp.474 |
TaWA 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 | Dephosphorylatio n[1] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 99.9972 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate CheYp TaWA
Product 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 |
TaWA 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[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. | 2 | Complexing[9] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 4 (uM^-1 s^-1) | 10 (s^-1) | Kd(bf) = 2.5(uM) | - | Substrate CheW TaA
Product 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 | 3 | Binding[11] | Chemotaxis Accession No. : 57 | Chemotaxis Pathway No. : 228 | 4 (uM^-1 s^-1) | 10 (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 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. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
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