December 1, 1985Journal of Biological ChemistryOpen Access

Kinetic mechanism of 1-N6-etheno-2-aza-ATP hydrolysis by bovine ventricular myosin subfragment 1 and actomyosin subfragment 1. The nucleotide binding steps.

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Population

Bovine cardiac myosin subfragment 1 (myosin-S1) and actomyosin subfragment 1 (actomyosin-S1)

Comparison

1-N6-etheno-2-aza-ATP (epsilon-aza-ATP) vs ATP and ADP

Design

Preclinical

Authors

SSSusan J. SmithUniversity of Cambridge HWHoward D. WhiteHeart Failure & Transplant

Discussion

Member takes

Implication

Epsilon-aza-ATP preserves key binding features in bovine myosin; leaves open its utility as a probe in human cardiac systems.

Structured PICO

Population

Bovine cardiac myosin subfragment 1 (myosin-S1) and actomyosin subfragment 1 (actomyosin-S1)

Intervention

1-N6-etheno-2-aza-ATP (epsilon-aza-ATP)

Comparator

ATP and ADP

Outcome

Kinetic mechanism of nucleotide binding and hydrolysis (rate constants and fluorescence enhancement)surrogate

The basic features of the nucleotide binding steps of bovine cardiac myosin remain unchanged when using epsilon-aza-ATP compared to ATP, despite quantitative differences in rate and equilibrium constants.

Cite This Study

Smith et al. (1985) studied this question.

synapsesocial.com/papers/6a76faade29fd788c9f6f7fc https://doi.org/10.1016/s0021-9258(18)95714-5

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