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Molecule Parameter List for CheYp

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

CheYp 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	7	2

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.

CheYp acting as a Molecule in  Chemotaxis Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
CheYp	Chemotaxis Accession No. : 57	Chemotaxis Pathway No. : 228	0.01	1.41	No
CheYp = 1.24e-07 M = 1.24e-01 uM As per Signal 22 in 1SIG_B.BCT provided by Matthew Levin CheYp = 1e-08 M = 1e-2 uM As per Set_Yp configuration in 1CONFIG.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

CheYp 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	Autodephosphoryl ation[1]	Chemotaxis Accession No. : 57	Chemotaxis Pathway No. : 228	0.037 (s^-1)	0 (s^-1)	-	-	Substrate CheYp Product CheY
	Autodephosphorylation of CheYp Kf = 3.7*10e-02 /sec Kb = 0 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475 Reaction Scheme 7
2	Dephosphorylatio n	Chemotaxis Accession No. : 57	Chemotaxis Pathway No. : 228	0.5 (uM^-1 s^-1)	0 (s^-1)	-	-	Substrate CheYp CheZ Product CheY
	CheZ stimulated dephosphorylation of CheYp Kf = 5*10e+05 /sec/M = 0.5 /sec/uM Kb = 0 /sec Bray et al 1993, Mol.Biol.Cell 4: 469-482 Table 2 pp.475 Reaction Scheme 8
3	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
4	Complexing[3]	Chemotaxis Accession No. : 57	Chemotaxis Pathway No. : 228	880.009 (uM^-1 s^-1)	55 (s^-1)	Kd(bf) = 0.0625(uM)	-	Substrate CheYp Motor Product MYp
	CheYp complexes with Flagellar Motor (M) Kf = 0.88/Set_Yp = 0.88/1e-08 /sec/M = 0.88e+2/sec/uM Kb = 5.5 /sec As per EXEC.C provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482
5	Complexing[4]	Chemotaxis Accession No. : 57	Chemotaxis Pathway No. : 228	2850 (uM^-1 s^-1)	66.4 (s^-1)	Kd(bf) = 0.0233(uM)	-	Substrate CheYp MYp Product MYpYp
	CheYp complexes with MYp Kf = 2.85/Set_Yp = 2.85/1e-08 /sec/M = 2.85e+2/sec/uM Kb = 6.64 /sec As per EXEC.C provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482
6	Complexing[5]	Chemotaxis Accession No. : 57	Chemotaxis Pathway No. : 228	6939.99 (uM^-1 s^-1)	51 (s^-1)	Kd(bf) = 0.0073(uM)	-	Substrate CheYp MYpYp Product MYpYpYp
	CheYp complexes with MYpYp Kf = 6.94/Set_Yp = 6.94/1e-08 /sec/M = 6.94e+2 /sec/uM Kb = 5.1 /sec As per EXEC.C provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482
7	Complexing[6]	Chemotaxis Accession No. : 57	Chemotaxis Pathway No. : 228	20069.7 (uM^-1 s^-1)	55 (s^-1)	Kd(bf) = 0.0027(uM)	-	Substrate CheYp MYpYpYp Product MYpYpYpYp
	CheYp complexes with MYpYpYp Kf = 20.07/Set_Yp = 20.07/1e-08 /sec/M = 20.07e+2 /sec/uM Kb = 5.5 /sec As per EXEC.C provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482

CheYp 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[ 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
2	Autophosphorylat ion[2]	Chemotaxis Accession No. : 57	Chemotaxis Pathway No. : 228	0 ()	0 (s^-1)	-	-	Substrate     - Product CheYp
	Autophosphorylation of CheY Paper says reaction not applicable Table 2 pp.475 Reaction Scheme 6 kf = 0/sec kb = 0/sec As per Reaction 14 in 1REACT.BCT provided by Matthew Levin Bray et al 1993, Mol.Biol.Cell 4: 469-482