This study delves into the physicochemical and pharmacokinetic properties of myricetin, a natural flavonoid compound, with a particular focus on its interaction with key biomolecules involved in inflammatory and enzymatic processes. The investigation begins by employing in silico methods to predict myricetin's Absorption, Distribution, Metabolism, Excretion, and Toxicity (ADMET) properties. These computational models reveal that myricetin exhibits a low gastrointestinal absorption rate and is not likely to permeate the blood-brain barrier. Furthermore, it shows interactions with specific cytochrome P450 enzymes, indicating potential metabolic pathways. Moving forward, the study explores myricetin's interactions with two pivotal biomolecules: Tumor Necrosis Factor-alpha (TNF-alpha) and Cyclooxygenase-2 (COX-2). Myricetin's binding to TNF-alpha demonstrates the potential to inhibit inflammatory responses, as evidenced by amino acid interactions involving GLY, LYS, PRO, ALA, and ILE, with a binding affinity of -5.04 Kcal/mol. Additionally, myricetin interacts with COX-2, indicating its ability to modulate prostaglandin production, vital in inflammation, pain, and fever regulation, with amino acid interactions involving ASN, HIS, ARG, LYS, VAL, and GLU and a binding affinity of -5.87 Kcal/mol. Finally, the study investigates myricetin's interaction with Matrix Metalloproteinase-13 (MMP-13) and Matrix Metalloproteinase-9 (MMP-9), crucial enzymes involved in the degradation of extracellular matrix components. Myricetin's interactions with these enzymes suggest its potential role in modulating tissue remodeling processes, with binding affinities of -6.03 Kcal/mol for MMP-13 and -3.64 Kcal/mol for MMP-9. Overall, this research sheds light on myricetin's physicochemical attributes, pharmaco kinetics, and its potential as a bioactive compound in modulating inflammatory and enzymatic processes, making it a promising candidate for further exploration in therapeutic applications.