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Molecule Parameter List for Tn

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
Tn participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000031

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
Chemotaxis57Pathway
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.

Tn acting as a Molecule in  
Chemotaxis Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
TnChemotaxis
Accession No. : 57
Chemotaxis
Pathway No. : 228
01.41No
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

Tn 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[1]Chemotaxis
Accession No. : 57
Chemotaxis
Pathway No. : 228
0.1
(uM^-1 s^-1)
1
(s^-1)
Kd(bf) = 10.0003(uM)-Substrate
CheW
Tn

Product
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.
2Binding[4]Chemotaxis
Accession No. : 57
Chemotaxis
Pathway No. : 228
0.05
(uM^-1 s^-1)
1
(s^-1)
Kd(bf) = 19.9999(uM)-Substrate
CheA
Tn

Product
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.
3Binding[10]Chemotaxis
Accession No. : 57
Chemotaxis
Pathway No. : 228
4
(uM^-1 s^-1)
10
(s^-1)
Kd(bf) = 2.5(uM)-Substrate
Tn
WA

Product
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.

Tn 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
BindingChemotaxis
Accession No. : 57
Chemotaxis
Pathway No. : 228
0.001
(uM^-1 s^-1)
1
(s^-1)
Kd(bf) = 1000.028(uM)-Substrate
Ni
Tar

Product
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



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