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Intrinsic regulation of substrate fluxes and energy conservation in Ca 2+ ‐ATPase
Author(s) -
de Meis Leopolde,
Inesi Giuseppe
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80756-0
Subject(s) - pi , substrate (aquarium) , enzyme , atpase , chemistry , biophysics , kinetic energy , endoplasmic reticulum , calcium atpase , biochemistry , physics , biology , classical mechanics , ecology
The Ca 2+ ‐ATPase of sarcoplasmic reticulum was utilized to demonstrate an intrinsic regulation of enzyme catalysis, whereby the ratio of forward and reverse flow is altered by the binding of Ca 2+ and P i to the enzyme. This is related to displacement of internal equilibria among intermediate enzyme ligand complexes, independent of the overall equilibrium of the ATP ⇌ ADP + P i transformation. A very high energy conservation with a velocity of reverse flow approaching that of forward flow, was obtained by increasing the enzyme affinity for P i in the presence of Me 2 SO.