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They catalyze the breakdown of molecules without the involvement of water and oxidizers, forming new bonds. Inadequate amounts may lead to disruptions in the metabolism of amino acids and organic acids. Therapeutic doses of enzymes are used to support metabolism and digestion.
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Lysases — are enzymes that catalyze the breaking of chemical bonds without the involvement of water. Unlike hydrolases and oxidoreductases, they facilitate the formation of double bonds or cycles, participate in the metabolism of carbohydrates, amino acids, and lipids, and also play a role in the synthesis of biomolecules. Their activity is important for maintaining energy balance and overall homeostasis in the body.

Definition and Classification

Lysases catalyze reactions of cleavage or addition of atom groups without hydrolysis. They act on different types of bonds — carbon, nitrogen, sulfur. The main subgroups are:

  • decarboxylases — remove carbon dioxide from molecules;
  • dehydrases — remove water molecules;
  • carbohydrate lyases — break carbohydrate bonds;
  • amino acid lyases — participate in reactions with amino acids.

Mechanisms of Action

The action of lyases is based on the formation of intermediate compounds that are processed into final products. They can:

  • remove or add functional groups;
  • form double bonds or cycles;
  • interact with coenzymes (for example, pyridoxal phosphate enhances the activity of certain lyases).

Role in Metabolism

Lysases are involved in the metabolism of carbohydrates, fats, and proteins, providing energy to the body.

Important functions include:

  • participation in the synthesis and breakdown of amino acids and fatty acids;
  • formation of neurotransmitters (for example, dopamine and serotonin through decarboxylases);
  • regulation of energy metabolism.

Applications in Medicine and Biotechnology

Lysases are used in the diagnosis and treatment of diseases, as well as in synthetic biology:

  • used in clinical tests to determine metabolite levels;
  • applied in the creation of biopharmaceuticals;
  • allow the synthesis of recombinant proteins and new biomolecules.

Enzymes used in therapy

Below are examples of enzymes from this class that are used in the treatment of various diseases:

Asparaginase. Enzyme from the lyase group that cleaves the amino acid asparagine. Used in oncology (especially in acute lymphoblastic leukemia) as tumor cells often depend on external asparagine. Administered by injection. The main downside is the possibility of allergic reactions and significant strain on the liver and pancreas.
Carbonic anhydrase. Although technically classified as hydrolases, its mechanism is closer to lyases. It participates in the reversible conversion of CO₂ and HCO₃⁻. Its inhibitors (acetazolamide) are used in clinical practice for the treatment of glaucoma, edema, metabolic alkalosis, and also in sports medicine for altitude adaptation.
Histidine-ammonia lyase. An enzyme involved in the conversion of histidine to urocanate. It has almost no direct therapeutic application in medicine, but is being studied as a marker of amino acid metabolism and in the context of skin diseases (the level of urocanic acid affects the barrier properties of the skin).
ADF-ribosylcyclase. Produces cyclic ADP-ribose derivatives that regulate calcium metabolism. Promising in research medicine — intracellular calcium control is important in neurological and cardiovascular disorders.
Fumaratliase. Catalyzes the reaction in the Krebs cycle (fumarate ⇌ malate). In clinical practice, the enzyme itself is not used, but its activity is considered in hereditary mitochondrial diseases (fumarase deficiency). Experiments are underway on enzyme replacement therapy.

Research and Prospects

Modern research is focused on understanding the structure and functions of lyases, as well as their use as biocatalysts.

Promising directions include:

  • development of new treatment methods for metabolic disorders;
  • application in the synthesis of complex organic compounds;
  • development of innovative pharmaceuticals.

The main challenges are related to the isolation and low stability of lyases under physiological conditions. This limits their widespread application.

It is expected that advancements in crystallography and molecular modeling methods will enable the creation of enzymes with improved properties, expanding their application possibilities in medicine, biotechnology, and industry.


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