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Molecule Parameter List for E1

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

E1 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.

E1 acting as a Molecule in SERCA Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
E1	SERCA Accession No. : 37	SERCA Pathway No. : 187	0	0.0016667	No
Intermediate from of Ca-ATPase (SERCA2a) which is ready to bind to first Ca.

E1 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
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.

E1 acting as a Product in a reaction in SERCA Network

Name	Accession Name	Pathway Name	Kf	Kb	Kd	tau	Reagents
reac1	SERCA Accession No. : 37	SERCA Pathway No. : 187	0.35 (s^-1)	0.35 (s^-1)	Keq = 1(uM)	1.429sec	Substrate E2 Product E1
kf and kb are the picked up from the Table-6 of literature source Mahaney et al. (2000 Mar) Biophys J. 78(3) 1306-23. .

Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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