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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 asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000011

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
SERCA37Pathway
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
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
CaE1SERCA
Accession No. : 37
SERCA
Pathway No. : 187
00.0016667No
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.
NameAccession NamePathway NameKfKbKdtauReagents
reac3SERCA
Accession No. : 37
SERCA
Pathway No. : 187
0.4
(s^-1)
0.4
(s^-1)
Keq = 1(uM)1.25secSubstrate
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.
NameAccession NamePathway NameKfKbKdtauReagents
reac2SERCA
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.



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