The effect of reaction temperature change on equilibrium 56621-48-8

From this literature《Molecular Mechanism for Isoform-Selective Inhibition of Acyl Protein Thioesterases 1 and 2 (APT1 and APT2)》,we know some information about this compound(56621-48-8)Name: 4-(Piperazin-1-yl)phenol, but this is not all information, there are many literatures related to this compound(56621-48-8).

Name: 4-(Piperazin-1-yl)phenol. So far, in addition to halogen atoms, other non-metallic atoms can become part of the aromatic heterocycle, and the target ring system is still aromatic. Compound: 4-(Piperazin-1-yl)phenol, is researched, Molecular C10H14N2O, CAS is 56621-48-8, about Molecular Mechanism for Isoform-Selective Inhibition of Acyl Protein Thioesterases 1 and 2 (APT1 and APT2).

Post-translational S-palmitoylation directs the trafficking and membrane localization of hundreds of cellular proteins, often involving a coordinated palmitoylation cycle that requires both protein acyltransferases (PATs) and acylprotein thioesterases (APTs) to actively redistribute S-palmitoylated proteins toward different cellular membrane compartments. This process is necessary for the trafficking and oncogenic signaling of S-palmitoylated Ras isoforms, and potentially other peripheral membrane proteins. Depalmitoylating enzymes APT1 and APT2 are sep. conserved in all vertebrates, suggesting unique functional roles for each enzyme. The recent discovery of APT isoform-selective inhibitors ML348 and ML349 has opened new possibilities to probe the function of each enzyme, yet it remains unclear how each inhibitor achieves orthogonal inhibition. Here, the authors report the high-resolution structure of human APT2 in complex with ML349 (1.64 Å), as well as the complementary structure of human APT1 bound to ML348 (1.55 Å). Although the overall peptide backbone structures are nearly identical, each inhibitor adopted a distinct conformation within each active site. In APT1, ML348 was positioned above the catalytic triad, but in APT2, the sulfonyl group of ML349 formed H-bonds with active site resident water mols. to indirectly engage the catalytic triad and oxyanion hole. Reciprocal mutagenesis and activity profiling revealed several differing residues surrounding the active site that served as critical gatekeepers for isoform accessibility and dynamics. Structural and biochem. anal. suggested that the inhibitors occupy a putative acyl-binding region, establishing the mechanism for isoform-specific inhibition, hydrolysis of acyl substrates, and structural orthogonality important for future probe development.

From this literature《Molecular Mechanism for Isoform-Selective Inhibition of Acyl Protein Thioesterases 1 and 2 (APT1 and APT2)》,we know some information about this compound(56621-48-8)Name: 4-(Piperazin-1-yl)phenol, but this is not all information, there are many literatures related to this compound(56621-48-8).

Reference:
Ether – Wikipedia,
Ether | (C2H5)2O – PubChem