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Molecule Parameter List for CaE1

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

CaE1 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	1	1

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
SERCA	37	Pathway	SERCA
All the constants are from: Mahaney JE. et al. Biophys J. (2000) 78(3) 1306-23. New Insights on cardiac Ca-ATPase (expressed in Sf21 cells) regulation by Phosphlamban.

CaE1 acting as a Molecule in  SERCA Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
CaE1	SERCA Accession No. : 37	SERCA Pathway No. : 187	0	0.0016667	No
1 Ca bond state of SERCA2a

CaE1 acting as a Substrate in a reaction in  SERCA 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
reac3	SERCA Accession No. : 37	SERCA Pathway No. : 187	0.4 (s^-1)	0.4 (s^-1)	Keq = 1(uM)	1.25sec	Substrate CaE1 Product CaE1_prime
kf and kb were taken form Table-6 of literature source ( Mahaney et al. ( 2000 Mar) Biophys J. 78(3) 1306-23.)

CaE1 acting as a Product in a reaction in  SERCA 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
reac2	SERCA Accession No. : 37	SERCA Pathway No. : 187	50 (uM^-1 s^-1)	120 (s^-1)	Kd(bf) = 2.4(uM)	-	Substrate Ca E1 Product CaE1
Kinetic constants for this step had substantial effects on the steady state EP level. For SERCA2a alone the kf was 200uM SERCA2a + Wild type Phospholamban kf was reduced to 100uM. SERCA2a + L37A Phospholamban kf was reduced to 50um as specified by the author ( Mahaney et al. (2000 Mar) Biophys J. 78(3) 1306-23.). kb in all the cases were maintained at 120/s.