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Abstract

Enzyme inhibitors play a crucial role in the treatment of various diseases by modulating the activity of specific enzymes involved in pathological processes. This review provides a comprehensive analysis of the structural and functional characteristics of enzyme inhibitors, emphasizing their therapeutic potential across a range of diseases. We first discuss the mechanisms by which enzyme inhibitors interact with their target enzymes, including competitive, non-competitive, and allosteric inhibition. The review then explores recent advancements in structural biology techniques, such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, which have enhanced our understanding of the binding interactions between inhibitors and their target enzymes. Additionally, we examine the functional implications of these interactions, including changes in enzyme activity and downstream signaling pathways. The review highlights key examples of enzyme inhibitors used in clinical practice, such as those targeting proteases in HIV/AIDS and kinases in cancer therapy, and discusses emerging inhibitors with potential for future therapeutic applications. By integrating structural and functional perspectives, this review aims to provide insights into the design of more effective enzyme inhibitors and the development of novel treatments for various diseases.