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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
Ta participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences2000042

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
Chemotaxis55Pathway
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
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
TaChemotaxis
Accession No. : 55
Chemotaxis
Pathway No. : 226
01.41No
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
TAChemotaxis
Accession No. : 55
Chemotaxis
Pathway No. : 226
1.551.41No
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.
 NameAccession NamePathway NameKfKbKdtauReagents
1Complexing[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.
2Complexing[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
3Binding[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.
4Binding[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.
 NameAccession NamePathway NameKfKbKdtauReagents
1Binding[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
2Binding[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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