Enzyme inhibitors
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Enzyme inhibitors are a class of substances that can specific binding to certain groups of enzymes and decrease their activity. By reducing or completely losing enzymes activity related to certain diseases in the organism, enzyme inhibitors can be used as related drugs to obtain curative effects.
Classification of enzyme inhibitors
Currently, as many as hundreds of enzyme inhibitors have been discovered.
- According to chemical properties
Enzyme inhibitors can be divided into inorganic compounds (such as heavy metal salts, chlorides, fluorides, phosphates, etc.) and organic compounds (such as isobutyric acid, urea derivatives, paraformaldehyde, etc.).
- According to inhibitor type
Enzyme inhibitors can be divided into oxidoreductase inhibitors, transferase inhibitors, hydrolase inhibitors, lyase inhibitors, isomerase inhibitors and synthetase inhibitors.
- According to the disease being treated
Enzyme inhibitors include anti-tumor enzyme inhibitors, anti-HIV enzyme inhibitors, anti-inflammatory enzyme inhibitors, anti-thrombotic enzyme inhibitors and so on.
- According to the mechanism of action with enzymes
Enzyme inhibitors can be divided into irreversible and reversible. Reversible inhibitors bind non-covalently and can dissociate from the enzyme, allowing the enzyme to regain activity once the inhibitor is removed. They are further classified into competitive, uncompetitive, and non-competitive inhibitors.
How do enzyme inhibitors work?
Irreversible inhibitors
Irreversible inhibitors covalently bind to the enzyme, permanently inactivating it. This binding usually occurs at the active site or a critical residue essential for enzyme activity. Irreversible inhibitors reduce the total number of active enzyme molecules, thereby decreasing Vmax. Km may remain unchanged if the remaining active enzymes function normally. Aspirin irreversibly inhibits cyclooxygenase-1 (COX-1) by acetylating a serine residue in the active site.
Competitive inhibitors
Competitive inhibitors resemble the substrate and compete for binding to the active site of the enzyme. By occupying the active site, they prevent the substrate from binding. This type of inhibition increases the apparent Km (the substrate concentration at which the reaction rate is half of Vmax) without affecting Vmax (the maximum reaction rate). The inhibition can be overcome by increasing substrate concentration. For example, methotrexate competes with dihydrofolate for the active site of dihydrofolate reductase.
Uncompetitive inhibitors
Uncompetitive inhibitors bind only to the enzyme-substrate complex, preventing the conversion of the substrate to the product. This binding typically occurs at a site distinct from the active site. Uncompetitive inhibition decreases both Km and Vmax, as the inhibitor only binds to the enzyme-substrate complex and not to the free enzyme. Lithium inhibits inositol monophosphatase in a manner consistent with uncompetitive inhibition.
Non-competitive inhibitors
Non-competitive inhibitors bind to an enzyme at a site other than the active site (allosteric site). This binding induces a conformational change in the enzyme that reduces its catalytic efficiency, regardless of substrate concentration. Non-competitive inhibition decreases Vmax without affecting Km. The inhibitor can bind to both the free enzyme and the enzyme-substrate complex. For example, cyanide inhibits cytochrome c oxidase by binding to a site other than the active site, blocking electron transport.
Source of enzyme inhibitors
Enzyme inhibitors are mainly derived from plants, microorganisms and chemical synthesis. The primary metabolites and secondary metabolites of microorganisms are able to produce enzyme inhibitors. Actinomycetes are the group of microorganisms that produce the most enzyme inhibitors. Bacteria and fungi are also crucial microbial sources of enzyme inhibitors. In addition to the traditional screening and isolation of medicinal bacteria, researchers have focused their attention on a variety of new microbial groups, such as marine microbes and extreme microbes. Plants are the main source of new drugs for enzyme inhibitors.
What do enzyme inhibitors do?
Enzyme inhibitors are vital to organisms. In animals and plants, there are biological macromolecular enzyme inhibitors related to human biological regulation. In industrial production, the quality of fermented products can be improved by inhibiting metabolic regulation enzymes. Enzyme inhibitors are widely used in agricultural production, medicine and military fields. Certain enzyme inhibitors could be taken as serve as herbicides or insecticides. Enzyme inhibitors could also be available for clinical applications. Lots of drugs and poisons related to diseases are enzyme inhibitors.
- Regulation of metabolic pathways
Enzyme inhibitors are crucial in the regulation of metabolic pathways. Cells use natural inhibitors to modulate enzyme activity, ensuring that metabolic processes occur at appropriate rates and in response to changing cellular conditions.
- Therapeutic agents
Many drugs are designed as enzyme inhibitors to treat diseases. By inhibiting specific enzymes, these drugs can modulate biochemical pathways and alleviate symptoms or cure diseases. Penicillin inhibits transpeptidase, an enzyme involved in bacterial cell wall synthesis. Protease inhibitors used in HIV therapy inhibit viral proteases necessary for virus replication. Inhibitors like imatinib target specific tyrosine kinases involved in cancer cell proliferation.
- Industrial applications
Enzyme inhibitors are used in various industrial processes to control enzyme activity. For example, inhibitors are added to food products to prevent enzymatic browning and spoilage.
