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Lyases are a class of enzymes that play a vital role in various biochemical processes by catalyzing the addition or removal of chemical groups in molecules, often resulting in the formation of double bonds or the cleavage of single bonds without hydrolysis or oxidation. These enzymes are essential for many metabolic pathways and have a wide range of applications in research and industry. Understanding the function and potential uses of lyases is critical to the advancement of several fields, including biotechnology, medicine, and environmental science. As an industry-leading supplier of enzymes, Creative Enzymes is pleased to offer a comprehensive range of high-quality lyases, with approximately 150 varieties, tailored to meet the diverse requirements of our customers.
Lyases are classified under EC (Enzyme Commission) number 4, which defines them as enzymes that facilitate the cleavage of bonds through mechanisms other than hydrolysis or oxidation. This process typically results in the formation of a new double bond or a new ring structure. In contrast to hydrolases, which break bonds using water, or oxidoreductases, which involve the transfer of electrons, lyases frequently remove groups from their substrates, leaving behind a double bond or, conversely, adding groups to a double bond.
The general reaction catalyzed by lyases can be represented as follows:
A-B → A + B
or
A + B → A-B
In this reaction, "A-B" represents the substrate molecule, which is either broken down into two products (A and B) or synthesized from two smaller molecules (A and B).
Lyases are classified into several subclasses based on the type of chemical bond they act upon. The major subclasses include:
Carbon-carbon lyases catalyze the cleavage of carbon-carbon bonds in a substrate. They are involved in a variety of metabolic processes, including the breakdown and synthesis of complex organic molecules. Decarboxylation reactions in which a carboxyl group is removed from a substrate, resulting in the formation of carbon dioxide and a new compound. A notable example is aldolase (e.g., 2-dehydro-3-deoxy-D-pentonate aldolase), which in glycolysis catalyzes the readily reversible splitting of fructose 1,6-bisphosphate (F-1,6-BP) into the products glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP). Carbon-carbon lyases are used in the synthesis of fine chemicals and pharmaceuticals, and in metabolic engineering to produce biofuels and other valuable compounds.
Fig. 1: The reaction that takes place in the second stage of glycolysis and catalyzed by aldolase.
Carbon-oxygen lyases catalyze the cleavage of carbon-oxygen bonds, often resulting in the formation of a new double bond or the addition of water to a double bond. An example is the dehydration of alcohols to alkenes or the hydration of alkenes to alcohols. Carbon-oxygen lyases are used in the food and beverage industry to produce flavors and aromas, and in the pharmaceutical industry for the synthesis of active pharmaceutical ingredients (APIs).
Carbon-nitrogen lyases catalyze the cleavage of carbon-nitrogen bonds commonly found in amino acids and other nitrogen-containing compounds. For example, the deamination of amino acids, in which an amino group is removed, resulting in the formation of a keto acid and ammonia (e.g., glucosamine-6-phosphate deaminase, aminodeoxyfutalosine deaminase). These enzymes are essential in the biosynthesis of amino acids, the degradation of nitrogenous compounds in wastewater treatment, and the development of diagnostic assays for various diseases.
Carbon-sulfur lyases catalyze the cleavage of carbon-sulfur bonds that are important in the metabolism of sulfur-containing compounds. A notable example is the cleavage of cysteine to pyruvate, ammonia, and hydrogen sulfide (e.g., D-cysteine desulfhydrase). Carbon-sulfur lyases are used in the bioremediation of sulfur-containing pollutants, the synthesis of sulfur-containing drugs, and the production of sulfur-based chemicals.
Carbon-halide lyases catalyze the cleavage of carbon-halide bonds found in halogenated organic compounds. The most common example is the dehalogenation of haloalkanes, resulting in the formation of alkanes and halide ions (e.g., haloalkane dehalogenase). These enzymes are used in the detoxification of halogenated environmental pollutants, the synthesis of halogen-free organic compounds, and the development of biocatalytic processes for the chemical industry.
Phosphorus-oxygen lyases catalyze the cleavage of phosphorus-oxygen bonds that are critical in the metabolism of nucleotides and other phosphorus-containing compounds. The most important example in cellular processes is the cyclization of ATP to cyclic AMP (cAMP) and pyrophosphate. Phosphorus-oxygen lyases are important in the study of signal transduction pathways, the development of anticancer drugs, and the production of cyclic nucleotide derivatives for research and therapeutic purposes.
Lyases have a wide range of applications across various fields, making them invaluable tools in both research and industry.
Lyases are essential tools in molecular biology and biotechnology:
Lyases play a critical role in drug development and manufacturing:
Lyases have significant applications in environmental protection and sustainability:
Lyases are widely used in the production and processing of food and beverages:
Lyases are a diverse and versatile class of enzymes that play a critical role in various biological processes and have numerous applications in research and industry. Their ability to catalyze the addition or removal of chemical groups without hydrolysis or oxidation makes them invaluable tools in fields such as pharmaceuticals, food production, environmental biotechnology, and molecular biology. Creative Enzymes is a trusted leader in the supply of enzymes, offering a diverse range of high-quality products. Explore our complete product catalog or contact us for custom enzyme blends tailored to your needs.
Catalog | Product Name | EC No. | CAS No. | Source | Price |
---|---|---|---|---|---|
NATE-0049 | Native Spinach Aldolase | EC 4.1.2.13 | 9024-52-6 | Spinach | Inquiry |
NATE-0048 | Native Rabbit Aldolase | EC 4.1.2.13 | 9024-52-6 | Rabbit muscle | Inquiry |
NATE-0024 | Native Porcine Aconitase | EC 4.2.1.3 | 9024-25-3 | Porcine heart | Inquiry |
NATE-0363 | Native E. coli 3-Deoxy-D-manno-octulosonate Aldolase | EC 4.1.2.23 | 9026-95-3 | E. coli | Inquiry |
NATE-0098 | Carbonic Anhydrase II from Human, Recombinant | EC 4.2.1.1 | 9001-03-0 | E. coli | Inquiry |
NATE-0097 | Native Human Carbonic Anhydrase I | EC 4.2.1.1 | 9001-03-0 | Human erythrocy... | Inquiry |
DIA-272 | Native Cystathionine-β-synthase | EC 4.2.1.22 | 9023-99-8 | Inquiry | |
DIA-225 | Native Human Neuron Specific Enolase | EC 4.2.1.11 | 9014-08-8 | Human brain | Inquiry |
DIA-212 | Native Microorganism Phosphoenolpyruvate carboxylase | EC 4.1.1.31 | 9067-77-0 | Microorganism | Inquiry |
DIA-182 | Native Microorganism N-Acetylneuraminic acid aldolase | EC 4.1.3.3 | 9027-60-5 | Microorganism | Inquiry |