What is a Lyase?
In physiology, Lyase meaning is defined as any member of an enzyme class that catalyzes the removal or addition of the elements of ammonia (nitrogen, hydrogen), carbon dioxide (carbon, oxygen), or water (oxygen, hydrogen) at double bonds in different ways other than hydrolysis and oxidation. For example, dehydrases remove water and decarboxylases remove carbon dioxide from amino acids.
Nomenclature
The systematic names can be formed as "substrate group-lyase." Common names are aldolase, dehydratase, decarboxylase, and so on. Synthase may be used in the name of a product when it is very essential, such as phosphosulfolactate synthase sulfite's Michael addition to phosphoenolpyruvate). A combination of both - a Michael and elimination addition is seen in the O-succinylhomoserine (thiol) -lyase (either MetY or MetZ) that catalyze first the γ-elimination of O-succinyl homoserine (succinate as a leaving group) and after that, the sulphide addition to the vinyl intermediate. First, this particular reaction was classified as a lyase, but then, it was reclassified as a transferase.
Examples of Lyase
A few examples of lyase include phenylalanine ammonia-lyase, citrate lyase, isocitrate lyase, hydroxynitrile, pectate lyase, argininosuccinate lyase, pyruvate formate lyase, alginate lyase, and pectin lyase.
Classification
In the classification of enzymes, lyases may be classified further into seven subclasses.
The first group includes Lyases that cleave carbon-carbon bonds and also include decarboxylases, aldehyde lyases by facilitating the aldol condensation's reverse reaction, oxo acid lyases (EC 4.1.3), which catalyzes the cleavage of several 3-hydroxy acids, including others.
The second one has a group of lyases, which break carbon-oxygen bonds like dehydratases. Hydro-lyases, being a part of carbon-oxygen lyases, may facilitate the cleavage of C-O bonds by water elimination. Phosphate reduction or the removal of alcohol from a polysaccharide was promoted by a few other carbon-oxygen lyases.
Lyases cleaving the carbon-nitrogen bonds are. And, they could release ammonia with the powerful cleaving ability and simultaneously produce a double ring or bond. A few of these enzymes may also help to eliminate an amide or amine group.
The fourth group shows lyases that split carbon-sulphur bonds that could either substitute or eliminate hydrogen sulphide (H₂S) from a reaction.
Carbon-halide bonds, by cleaving enzymes, are the lyases in the fifth group and which utilize an action mode, which removes hydrochloric acid from dichloro-diphenyl-trichloroethane (DDT), a synthetic pesticide.
Sixth group comprises the bonds of lyases fracturing phosphorus-oxygen, such as guanylyl cyclase and adenylyl cyclase, and they eliminate phosphate from the nucleotide triphosphates.
Example of Lyases in Each Category
Carbon-Carbon Lyases
Carboxy-Lyases: Pyruvate decarboxylase, acetoacetate decarboxylase, Oxaloacetate decarboxylase, Glutamate decarboxylase, Malonyl-CoA decarboxylase, Ornithine decarboxylase, Phosphoribosylaminoimidazole carboxylase, Lysine decarboxylase, Histidine decarboxylase, Aromatic L-amino acid decarboxylase, Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase, Phosphoenolpyruvate carboxylase, Uroporphyrinogen III decarboxylase, Pyrophosphomevalonate decarboxylase, RUBISCO, Adenosylmethionine decarboxylase, phosphoenolpyruvate carboxykinase
Aldehyde-Lyases: 2-hydroxyphytanoyl-CoA-lyase, aldolase A, aldolase B
Oxo-Acid-Lyases: 3-hydroxy-3-methylglutaryl-CoA lyase
Carbon-Oxygen Lyases: Fumarase, carbonic anhydrase, Enolase (Alpha), aconitase, Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase, Methylglutaconyl-CoA hydratase, Tryptophan synthase, Porphobilinogen synthase, cystathionine beta-synthase, 3-isopropyl malate dehydratase, nitrile hydratase, Urocanate hydratase, Uroporphyrinogen III synthase.
Carbon-Nitrogen Lyases:
Ammonia-Lyases: Histidine ammonia-lyase, Formiminotransferase cyclodeaminase, Serine dehydratase
Amidine-Lyases: Argininosuccinate lyase, Adenylosuccinate lyase
Carbon-Sulphur Lyases: Cystathionine gamma-lyase, Cystathionine-beta-lyase, Leukotriene C4 synthase
Carbon-Halide Lyases: Dichloromethane dehalogenase, Halohydrin dehalogenase
Phosphorus-Oxygen Lyases: guanylate cyclase, adenylate cyclase
Substrate Specificity
Usually, the specificity of a narrow substrate is considered to be a drawback for any enzyme's commercialization because it greatly restricts the enzyme's flexibility as an assistant in the related compound's production. Generally, lyases, but not all the time, are found with narrow substrate specificity. Most of the ammonia and hydratases-lyases possess a quite narrow substrate specificity, whereas the substrate specificity for decarboxylases, oxy nitrilases, and aldolases is much broader.
Note that the substrate specificity of a particular lyase varies based on its source. However, it is not given as an absolute prerequisite for enzymes to own the unrestricted substrate specificity for their commercial exploitation. Also, there are many lyases in commercial use bearing a narrow substrate spectrum.
Co-factor Requirements
The enzyme's commercial potential may be severely limited by the expensive cofactor's requirement. Since the addition catalyzed by lyase does not implicate the mere reduction or oxidation, it is not an important requirement for cofactors. However, till now, many lyases identified do require cofactors that are involved in the stabilization of reaction intermediates, substrate binding, substrate polarisation, temporary binding of the nucleophile, and more.
The majority of these cofactors are covalently bound to the enzyme and are not very expensive. Thereby, the lyases' cofactors do not establish a barrier to their commercialization. The requirements for lyases' cofactors differ as per their different sources.
Lyase Deficiency Disorder
Lyase deficiency, which is also referred to as HMG-CoA lyase deficiency, is given as a rare inherited disorder, which causes a mess in the metabolism of amino acid leucine and also prevents the body from synthesizing ketones, which are used for energy production during the body's food lacking periods. This condition could be inherited in an autosomal recessive pattern, which means that both copies of the gene in every cell undergo mutations.
Usually, the lyase deficiency symptoms express within the life's first year and primarily include vomiting, diarrhea, dehydration, lethargy, and weak muscular development. During the lyase deficiency episode, blood sugar concentrations may be either extremely low or hypoglycemic and a few harmful compounds would be accumulated to cause the blood to become quite acidic.
Whereas, if it is left untreated, the disorder could even initiate convulsions, coma, breathing problems, and also death. Infection, strenuous exercise, and other physical stresses may probably give rise to bouts with the symptoms of lyase deficiency.
FAQs on Lyase
1. How to relieve lyase deficiency disorder?
The lyase deficiency symptoms would be amplified after going long periods with no food ingestion. Thus, people attacked with this specific disease should be ensured with regular ingestion and good balance. Intaking foods that are low in protein, rich in carbohydrates and fat may be beneficial to prevent low blood sugar levels. In addition, L-Carnitine can aid in the production of cellular energy, which would be extremely beneficial when the body is dehydrated and lethargic.
2. What are hydrolases?
Hydrolase is defined as a class of an enzyme that commonly performs as biochemical catalysts that use water in a chemical bond breakage that typically results in dividing a larger molecule into smaller molecules. In short, these words utilize water molecules to break complex molecules into their simplest forms, for example, the enzyme sucrase uses water and breaks down sucrose into both fructose and glucose. Thus, this class of enzymes is widely used in various metabolic reactions occurring in the human body, thereby performing a wide variety of functions in the body.
3. Explain lyases with an example?
Lyases will split the molecule without the addition of water. For example, aldolase A splits fructose-1 and 6-bisphosphate to dihydroxyacetone phosphate and glyceraldehyde-3- phosphate without adding any water. They frequently add a new ring structure or generate a double bond. One example is the lyase, which acts on ATP to produce cAMP and PPi. One of the distinguishing features of a lyase is that it requires one substrate for the reaction in one direction and two substrates for the reaction in the opposite direction (referred to as Michael addition). Decarboxylases, aldolases, and dehydratases are examples of lyases.
4. Elaborate on the classification of lyases along with their examples.
Lyases constitute group four of enzyme classification. The enzymes included in the lyase group can further be divided into six sub-categories depending upon the bond on which they are acting. The first sub-category of lyases includes enzymes that act on the carbon-carbon bonds between atoms. This class includes a wide range of enzymes like carboxylases (oxaloacetate, ornithine decarboxylase, pyruvate decarboxylase), aldehyde-lyases (aldolase A and B, 2-hydroxyphytanoyl-CoA-lyase), and oxo-acid-lyases (3-hydroxy-3-methylglutaryl-CoA lyase). The second sub-category of lyases includes enzymes that act on the carbon-oxygen bond, for example, carbonic anhydrase, aconitase, fumarase, nitrile hydratase. The third sub-category of enzymes includes enzymes that act on the carbon-nitrogen bond, for example, ammonia lyases (serine dehydratase, histidine ammonia-lyase) and amidine lyases (adenylosuccinate lyase and argininosuccinate lyase). The fourth sub-category of lyases include enzymes acting on carbon-sulphur bonds, for example, C4 synthase, cystathionine beta lyase, and gamma lyases). The fifth sub-category of lyases includes enzymes that cleave carbon-halide bonds, for example, halohydrin dehalogenase and dichloromethane dehalogenase. The last sub-category of lyases includes enzymes that act on phosphorus oxygen bonds, for example, guanylate cyclase and adenylate cyclase.
5. Explain Hydrolases with an Example?
Hydrolases refer to a class of enzymes that acts as a biochemical catalyst that uses water to break down a complex molecule into its simplest form. Hydrolases are the ones that split the molecule by the addition of water. Examples of Hydrolase are: sucrose can be hydrolyzed into both glucose and fructose by adding water in the presence of enzyme sucrase. Therefore, the sucrase enzyme is an example of hydrolases that uses water to break down sucrose into both glucose and fructose.