Background:

2,3-Butanedione-2-monoxime is a myosin ATPase inhibitor.

Myosin, an ATPase, can convert chemical energy into directed movement and is regarded as a molecular motor. Myosin has various shapes and sizes. More than 11 myosin classes have been identified, and more will be found. The common feature of all of these molecules is a section close to the N terminus, which can be identified as a motor domain.

In vitro: 2,3-Butanedione-2-monoxime (BDM), a general probe of myosin function, was widely used in muscle research as a low-affinity but specific chemical phosphatase that could reversibly inhibit the myosin cross-bridge cycle. It was found that wild-type cells treated with BDM at 20 mM for around two generation times were smaller than untreated controls and showed a septation index about twice that observed in the absence of the inhibitor. Moreover, the organization of actin at the cell poles was disorganized in the presence of BDM, however, cells formed a cytokinetic actin ring. In addition, when nitrogen-starved stationary-phase cells were reinoculated into fresh medium in the presence of BDM, the time taken to repolarize the actin cytoskeleton and to resume the characteristic vegetative cell shape were both delayed substantially [1].

In vivo: So far, there is no animal in vivo data reported.

Clinical trial: So far, no clinical study has been conducted.

Reference:
[1] May KM, Wheatley SP, Amin V, Hyams JS.  The myosin ATPase inhibitor 2,3-butanedione-2-monoxime (BDM) inhibits tip growth and cytokinesis in the fission yeast, Schizosaccharomyces pombe. Cell Motil Cytoskeleton. 1998;41(2):117-25.