In Silico Evaluation of Bioactive Compounds from Sungkai Leaves (Peronema canescens Jack) as Potential Allosteric Activators of Catalase (CAT)

Reactive oxygen species (ROS) are highly reactive molecules produced during normal metabolism that can cause oxidative stress when accumulated. Catalase (CAT) is a key antioxidant enzyme that decomposes hydrogen peroxide into water and oxygen, maintaining cellular redox balance. This study investigated bioactive compounds from Peronema canescens (Sungkai) leaves as potential allosteric activators of catalase using an integrated in silico approach. Forty-three phytochemicals were evaluated through ADMET profiling, toxicity prediction, and molecular docking against the catalase allosteric site. Global and local reactivity descriptors, structure–activity relationships (SAR), and bioactivity radar analyses were applied to assess drug-likeness and pharmacological potential. Among the tested ligands, SMR000036195 (2-oxo-6-(piperidin-1-sulfonyl)-benzothiazole-3-carboxylic acid isobutyl ester) exhibited the strongest binding affinity (–7.63 kcal/mol), surpassing the reference activator D-trehalose (–6.07 kcal/mol). The compound also demonstrated favourable pharmacokinetic and safety profiles, suggesting low toxicity and good bioavailability. Key residue interactions indicated stable allosteric binding that may enhance catalase activity through conformational modulation. These findings propose SMR000036195 as a promising natural allosteric activator of catalase, potentially contributing to the development of antioxidant therapies targeting oxidative stress–related disorders. Further in vitro and in vivo studies are warranted to validate its enzyme activation and therapeutic potential.