Results 301 to 310 of about 697,459 (324)
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Enzymatic hydrolysis of ATP and e-ATP by F-actin

Journal of Bioenergetics and Biomembranes, 1976
Enzymatic hydrolysis of e-ATP by F-actin with and without application of sonic vibration at various pHs was investigated and compared with that of ATP. There was no significant difference on enzymatic activity between F-actin-bound e-ADP and F-actin-bound ADP. The hydrolysis rate of e-ATP under sonic vibration decreases monotonically with decreasing pH,
H, Asai, M, Asai
openaire   +2 more sources

Mechanism of ATP hydrolysis

1982
In searching for the molecular basis of contraction we need to relate chemical events with mechanical events. These must be quantitatively coupled in their extent (thermodynamics) and time course (kinetics). Unfortunately, chemical kinetic analysis of muscle itself presents practical and theoretical difficulties. In a muscle fibre the interaction sites
openaire   +1 more source

Cobalt(III)-promoted hydrolysis of atp

Journal of Inorganic Biochemistry, 1984
Abstract The rate of phosphate hydrolysis of ATP in the substitution-inert complex Co(NH3)4ATP-has been examined in the presence and absence of [Co(cyclen)(H2O)2]3+. The rate of hydrolysis of Co(NH3)4ATP- in the absence of [Co(cyclen)(H2O)2]3+ is essentially independent of pH in the range 6.0 to 9.0, and the rate constant is 2.6 × 10−5 sec −1 at pH 9.
Gene R. Meyer, Richard Cornelius
openaire   +1 more source

Coupling ATP hydrolysis to mechanical work

Nature Cell Biology, 1999
Kinesin is a molecular motor that works as a cellular ‘porter’. Its job is to walk along microtubules, carrying membrane-bound bags of chemicals. To do this it must convert the chemical energy of ATP into mechanical work, and ATP hydrolysis may be very tightly coupled to the number and length of steps taken by kinesin.
Alex E. Knight, Justin E. Molloy
openaire   +1 more source

Modulation of MutS ATP Hydrolysis by DNA Cofactors

Biochemistry, 2000
Escherichia coli MutS protein, which is required for mismatch repair, has a slow ATPase activity that obeys Michalelis-Menten kinetics. At 37 degrees C, the steady-state turnover rate for ATP hydrolysis is 1.0 +/- 0.3 min(-1) per monomer equivalent with a K(m) of 33 +/- 6 microM.
K P, Bjornson, D J, Allen, P, Modrich
openaire   +2 more sources

Regulation of ATP hydrolysis in hepatoma 22a mitochondria

Archives of Biochemistry and Biophysics, 1991
A decrease in the rate of ATP hydrolysis was observed after preincubation of intact mitochondria from hepatoma 22a with an uncoupler. This effect is due both to a decrease in the rate of ATP transport and to an inactivation of the F0F1-ATPase. The former effect is shown to result from an uncoupler-induced ADP efflux.
B V, Chernyak   +2 more
openaire   +2 more sources

The mechanism of ATP hydrolysis by sarcoplasmic reticulum

Archives of Biochemistry and Biophysics, 1975
Abstract Quench-flow kinetic studies of the rate of formation and decomposition of phosphoprotein by the [Mg 2+ + Ca 2+ ] activated ATPase of sarcoplasmic reticulum indicate that the rate limiting step of ATP cleavage is the hydrolysis of phosphoprotein.
R L, Coffey   +3 more
openaire   +2 more sources

Hypothesis for Coupling Energy Transduction with ATP Synthesis or ATP Hydrolysis

Nature New Biology, 1971
A mechanistic hypothesis for coupling and energy transduction has been developed. It is suggested that membrane-bound ATPases play an intermediate high energy role.
openaire   +2 more sources

MCC950 directly targets the NLRP3 ATP-hydrolysis motif for inflammasome inhibition

Nature Chemical Biology, 2019
Rebecca C. Coll   +10 more
semanticscholar   +1 more source

Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM

Nature Structural & Molecular Biology, 2018
F. Merino   +7 more
semanticscholar   +1 more source

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