Related Experiment Video
Updated: Aug 29, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
Published on: April 29, 2022
Peptidyl aldehydes as slow-binding inhibitors of dual-specificity phosphatases
Junguk Park1, Hua Fu, Dehua Pei
1Department of Chemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH 43210, USA.
Abstract:
Peptidyl aldehydes were tested for inhibition of dual-specificity phosphatases VH1 and VHR. The most potent compound, cinnamaldehyde-Gly-Glu-Glu (Cinn-GEE), acted as a slow-binding inhibitor with K(I)* values of 18 and 288 microM against VH1 and VHR, respectively.
Related Concept Videos
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Allosteric Regulation
Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...
Enzyme Inhibition
Phosphoinositides and PIPs
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

