Perspective - Journal of Biochemistry and Biotechnology (2023) Volume 6, Issue 3
Unveiling the Power of Enzyme Inhibitors: Paving the Way for Therapeutic Innovations
Denriette Harkas *
Department of Medicine, Taipei Medical University-Shuang Ho Hospital, Taipei, Taiwan .
- *Corresponding Author:
- Denriette Harkas
Department of Medicine
Taipei Medical University-Shuang Ho Hospital
Taiwan
E-mail: harkas@denriette.hu
Received:30-May-2023,Manuscript No. AABB-23-104224;Editor assigned: 02-Jun-2023, PreQC No. AABB-23-104224(PQ);Reviewed:16-Jun-2023, QC No. AABB-23-104224;Revised:20-Jun-2023, Manuscript No. AABB-23-104224 (R); Published:29-Jun-2023, DOI:10.35841/aabb-6.3.143
Citation: Harkas D. Unveiling the power of enzyme inhibitors: Paving the way for therapeutic innovations. J Biochem Biotech 2023;6(3):143
Introduction
Enzymes are essential biological molecules that catalyze and regulate countless biochemical reactions within living organisms. However, there are instances when modulating or inhibiting specific enzyme activities becomes crucial, particularly in the context of disease treatment. Enzyme inhibitors, small molecules or biologics that selectively bind to enzymes, have revolutionized modern medicine by providing valuable tools for understanding enzyme function and offering innovative therapeutic strategies. In this article, we delve into the world of enzyme inhibitors, exploring their mechanisms, classifications, and significant contributions to medical research and drug development [1].
Mechanisms of enzyme inhibition
Enzyme inhibitors exert their effects by interfering with key steps in enzyme catalysis. These mechanisms can be broadly categorized into two types: reversible inhibition and irreversible inhibition. Reversible inhibition: In reversible inhibition, the binding of the inhibitor to the enzyme is temporary and can be readily dissociated. This form of inhibition can be further classified into three types: Competitive inhibition: Competitive inhibitors compete with the substrate for the active site of the enzyme. By binding to the active site, they prevent the substrate from interacting with the enzyme, thus reducing enzymatic activity. Increasing substrate concentration can overcome competitive inhibition. Non-competitive inhibition: Non-competitive inhibitors bind to a site distinct from the active site, termed the allosteric site. This binding induces a conformational change in the enzyme, impairing its catalytic activity. Non-competitive inhibitors do not compete with the substrate and cannot be overcome by increasing substrate concentration [2].
Uncompetitive inhibition
Uncompetitive inhibitors bind to the enzyme-substrate complex, preventing the release of the product. This type of inhibition requires both substrate and inhibitor to be present, and it decreases the effective concentration of the enzyme-substrate complex. Irreversible inhibition: Irreversible inhibitors form stable covalent bonds with the enzyme, resulting in permanent inactivation. Unlike reversible inhibitors, irreversible inhibitors cannot be easily reversed or overcome. They often exhibit a high degree of selectivity, making them valuable tools in targeted therapy [3].
Significance in medical research and drug development
Enzyme inhibitors have significantly impacted medical research and drug development, offering diverse opportunities for therapeutic intervention. Here are a few notable contributions: Targeted cancer therapy: Enzyme inhibitors have revolutionized cancer treatment by specifically targeting enzymes involved in tumor growth, angiogenesis, and metastasis. For example, tyrosine kinase inhibitors (TKIs) target abnormal kinase activity in cancer cells, inhibiting their growth signaling pathways. These inhibitors have been successful in treating various cancers, such as chronic myeloid leukemia (CML) and non-small cell lung cancer (NSCLC). Treatment of infectious diseases: Enzyme inhibitors have played a vital role in developing drugs against infectious diseases. Protease inhibitors, commonly used in antiviral therapy, block the enzymatic activity of viral proteases, preventing viral replication. This approach has been successful in managing HIV/AIDS and hepatitis C infections [4].
Enzyme replacement therapy:
In certain diseases, such as lysosomal storage disorders, where specific enzymes are deficient or defective, enzyme replacement therapy (ERT) utilizes recombinant enzymes or their analogs to restore normal function. By providing exogenous enzymes, ERT aims to alleviate symptoms and improve the quality of life for affected individuals. Understanding enzyme function: Enzyme inhibitors serve as valuable tools for deciphering the intricate mechanisms of enzyme function. By selectively inhibiting specific enzymes, researchers can investigate their roles in normal physiology and disease processes, providing insights for future therapeutic interventions.[5].
Conclusion
The last paper in this Special Issue is a review of the characteristics of food-protein-derived antidiabetic bioactive peptides. The authors provide an overview of the DPP-IV, PTP-1B, and α-glucosidase inhibitors and updated information on the methods used for the discovery of DPP-IV inhibitory peptides released from food protein hydrolysate, since the inhibition of all these enzymes is promising for the treatment of diabetes type 2.
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