Akademik Veri Yönetim Sistemi
International Eurasian Conference on Biotechnology and Biochemistry (BioTechBioChem 2020), Ankara, Türkiye, 16 - 18 Haziran 2020, ss.216
Abstract
Enzymes are biological catalysts, mostly in the protein structure, that catalyse chemical reactions in living things. It is possible to interfere with any metabolic pathway by increasing or decreasing the activities of enzymes. Recently, scientists have recognized enzymes as the most attractive targets for small molecule drug intervention in human diseases. Enzymes are often the primary molecular targets of drug search efforts. Much of the information driving these medicinal chemistry efforts comes from in vitro evaluation of enzyme-inhibitor interactions. Therefore, it is important to correctly identify the type of inhibition. Enzyme inhibitors are low molecular weight chemical compounds that reduce or permanently (irreversibly) inhibit the enzyme's catalytic activity. Irreversible inhibitors that are covalently bound to the enzyme provide an alternative and complementary way to elucidate functional groups in the enzyme active region so they limit competition with high concentrations of endogenous ligands and achieve desired pharmacological effects even at lower drug concentrations/doses. Or, in cases where the cellular substrate concentration is high, enzyme inhibitors that work with non-competitive inhibition are ideal for disrupting enzyme targets in metabolic pathways because the accumulation of the substrate cannot prevent inhibition owing to the fact that it is not competing. In enzymes, the active site is more protected than the allosteric site, and a mutation in this region is a low probability to resist inhibition. Therefore, competitive inhibition with an inhibitor that is structurally similar to the substrate can often be preferred in the treatment of many diseases. The purpose of this presentation is to give an overview of enzyme inhibition, application of enzyme inhibition in the clinic, and examples of drugs targeting enzymes.