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Molecule Parameter List for CheA

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

CheA participated as	Molecule	Sum total of	Enzyme	Substrate of an enzyme	Product of an enzyme	Substrate in Reaction	Product in Reaction
No. of occurrences	1	0	0	0	0	10	2

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.

CheA acting as a Molecule in  Chemotaxis Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
CheA	Chemotaxis Accession No. : 55	Chemotaxis Pathway No. : 226	1.13	1.41	No
CheA = 1.13e-06 M = 1.13 uM As per Signal in 1SIG_B.BCT provided by Matthew Levin CheA = 4250 molecules per cell As per Enzyme entry 4 in 1ENZ.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

CheA 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	Autophosphorylat ion	Chemotaxis Accession No. : 55	Chemotaxis Pathway No. : 226	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. : 55	Chemotaxis Pathway No. : 226	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. : 55	Chemotaxis Pathway No. : 226	1 (uM^-1 s^-1)	0 (s^-1)	-	-	Substrate CheA TnWA Product CheAp
	Aspartate bound Tar and CheW complex TaW = 0 M As per Signal 7 in 1SIG_B.BCT Cell volume = 1.41e-15 L Table 1 pp.474 Bray et al 1993, Mol.Biol.Cell 4: 469-482
4	Binding[2]	Chemotaxis Accession No. : 55	Chemotaxis Pathway No. : 226	0.4 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 2.5(uM)	-	Substrate CheA TW Product TWA
	MYpYpYpYp = 1.51e-09 M = 1.51e-3 uM As per Signal 27 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
5	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
6	Binding[4]	Chemotaxis Accession No. : 55	Chemotaxis Pathway No. : 226	0.05 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 19.9999(uM)	-	Substrate CheA Tn Product TnA
	Bias calculated as per formula stated on pp.471 Bias = [M + MYp] / [M + MYp + MYpYp + MYpYpYp + MYpYpYpYp] Bray et al 1993, Mol.Biol.Cell 4: 469-482 Initialy set to 0.7
7	Binding[5]	Chemotaxis Accession No. : 55	Chemotaxis Pathway No. : 226	0.4 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 2.5(uM)	-	Substrate CheA TnW Product TnWA
	MYp = 9.53*e-10 M = 9.53*e-4 uM As per Signal 24 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
8	Binding[6]	Chemotaxis Accession No. : 55	Chemotaxis Pathway No. : 226	0.4 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 2.5(uM)	-	Substrate CheA TaW Product TaWA
	Motor = 8.5 molecules per cell As per Enzyme entry 7 in 1ENZ.BCT provided by Matthew Levin Motor = 6.73e-9 M = 6.73e-3 uM As per Signal 23 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
9	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.
10	Complexing[10]	Chemotaxis Accession No. : 55	Chemotaxis Pathway No. : 226	0.05 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 19.9999(uM)	-	Substrate CheA CheW Product WA

CheA 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	Phosphotransfer	Chemotaxis Accession No. : 55	Chemotaxis Pathway No. : 226	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. : 55	Chemotaxis Pathway No. : 226	0.27 (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