SIRT2 Inhibitors

AGK2 is a selective SIRT2 inhibitor that disrupts the enzyme's deacetylation activity by binding to its active site, leading to altered protein interactions and cellular signaling pathways. This compound exhibits unique kinetic properties, demonstrating a competitive inhibition mechanism that affects substrate affinity. AGK2's distinct molecular interactions can modulate cellular processes, influencing the dynamics of protein acetylation and contributing to the regulation of various metabolic functions.

Sirtinol acts as a selective inhibitor of SIRT2, engaging in unique molecular interactions that stabilize its binding to the enzyme's active site. This compound alters the conformational dynamics of SIRT2, impacting its deacetylation activity and influencing downstream signaling cascades. Sirtinol's distinct reaction kinetics reveal a non-competitive inhibition profile, which modifies substrate turnover rates and affects the overall balance of acetylation within cellular environments.

A small molecule that might inhibit SIRT2 deacetylase activity, potentially impacting cell cycle regulation and tumor growth.

Cambinol serves as a selective inhibitor of SIRT2, exhibiting a unique binding affinity that disrupts the enzyme's structural integrity. This compound interacts with specific residues within the active site, leading to altered enzyme dynamics and reduced catalytic efficiency. Cambinol's inhibition mechanism is characterized by a mixed-type inhibition, influencing both substrate binding and turnover. Its distinct physicochemical properties facilitate targeted interactions, impacting cellular acetylation states.

A small molecule that might inhibit SIRT2 deacetylase activity, potentially impacting cell cycle regulation and cancer grow

BML-266 is a selective SIRT2 inhibitor that engages in unique molecular interactions, primarily through hydrophobic and hydrogen bonding with key amino acid residues in the enzyme's active site. This compound alters the conformational landscape of SIRT2, resulting in a significant decrease in its deacetylation activity. The kinetic profile of BML-266 reveals a competitive inhibition mechanism, effectively modulating substrate affinity and influencing downstream signaling pathways. Its distinct structural features enhance specificity, making it a notable player in the regulation of cellular processes.

SIRT1/2 Inhibitor VII is a potent SIRT2 inhibitor characterized by its ability to disrupt enzyme-substrate interactions through specific steric hindrance. This compound exhibits a unique binding affinity, stabilizing an inactive conformation of SIRT2 that impedes its catalytic function. The inhibitor's kinetic behavior suggests a non-competitive inhibition model, influencing the enzyme's activity without directly competing with the substrate. Its structural attributes contribute to its selectivity, impacting various cellular mechanisms.

A potential SIRT2 inhibitor that might target its deacetylase activity, potentially affecting cellular processes and cancer cell growth.

B2 functions as a selective SIRT2 inhibitor, exhibiting unique molecular interactions that alter the enzyme's conformational dynamics. By engaging in specific hydrogen bonding and hydrophobic interactions, B2 effectively stabilizes a closed conformation of SIRT2, thereby inhibiting its deacetylation activity. The compound's reaction kinetics reveal a mixed inhibition pattern, suggesting that it can modulate SIRT2 activity through both competitive and allosteric mechanisms, influencing downstream signaling pathways.

SIRT2 Inhibitor, Inactive Control, serves as a structural analog that mimics the substrate binding site of SIRT2, yet lacks the ability to elicit a biological response. Its presence can disrupt the enzyme's normal substrate interactions, leading to altered enzyme kinetics. This compound showcases unique steric hindrance properties, which can influence the spatial arrangement of SIRT2's active site, potentially affecting the enzyme's overall stability and function in cellular processes.