Type I 4-phoshatase α Inhibitors

The chemical class of Type I 4-phosphatase α inhibitors would include a wide range of compounds, given the lack of specificity of the term "Type I 4-phosphatase α." In general, phosphatase inhibitors function by either mimicking the transition state of the enzyme's natural substrate, chelating necessary metal ions in the active site, or binding to active site residues to prevent catalysis.

Inhibitors like sodium orthovanadate and sodium fluoride act by mimicking phosphate groups or by forming complexes with catalytic metal ions. Cantharidin and calyculin A are natural toxins that inhibit protein phosphatases through covalent modification or by binding tightly to the active site. Okadaic acid and microcystin-LR, both produced by marine organisms, are potent inhibitors of PP2A and PP1, often used in research to study cellular phosphorylation processes. Tautomycetin is a more selective inhibitor that allows for differential inhibition of phosphatases.