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Molecule Parameter List for CheAp

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
CheAp participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000023

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.

CheAp acting as a Molecule in  
Chemotaxis Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
CheApChemotaxis
Accession No. : 57
Chemotaxis
Pathway No. : 228
0.5691.41No
CheAp = 5.69e-07 M = 5.69e-1 uM As per Signal entry 17 in 1SIG_B.BCT Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482

CheAp 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
1PhosphotransferChemotaxis
Accession No. : 57
Chemotaxis
Pathway No. : 228
1
(uM^-1 s^-1)
0
(uM^-1 s^-1)
--Substrate
CheAp
CheB

Product
CheA
CheBp
  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
2
  • Phosphotransfer[
    1]
  • Chemotaxis
    Accession No. : 57
    Chemotaxis
    Pathway No. : 228
    0.263
    (uM^-1 s^-1)
    0
    (uM^-1 s^-1)
    --Substrate
    CheAp
    CheY

    Product
    CheA
    CheYp
      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

    CheAp 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
    1
  • Autophosphorylat
    ion
  • Chemotaxis
    Accession No. : 57
    Chemotaxis
    Pathway No. : 228
    0.001
    (s^-1)
    0
    (s^-1)
    --Substrate
    CheA

    Product
    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
    2
  • Autophosphorylat
    ion[1]
  • Chemotaxis
    Accession No. : 57
    Chemotaxis
    Pathway No. : 228
    0.0757
    (uM^-1 s^-1)
    0
    (s^-1)
    --Substrate
    CheA
    TWA

    Product
    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
    3
  • Autophosphorylat
    ion[3]
  • Chemotaxis
    Accession No. : 57
    Chemotaxis
    Pathway No. : 228
    1
    (uM^-1 s^-1)
    0
    (s^-1)
    --Substrate
    CheA
    TnWA

    Product
    CheAp
      TnWA stimulated autophosphorylation of CheA TnWA is complex of Tar, CheW, CheA and Ni Kf = 1*10e+06 /sec/M = 1 /sec/uM Kb = 0 /sec As per Reaction 10 in 1REACT.BCT provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475, Reaction scheme 3



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