Isomerases

Isomerases are enzymes that catalyse processes that transfer functional groups inside a molecule, resulting in the formation of isomeric forms.: Alanine racemase is responsible for catalysing the conversion of L-alanine into its isomeric form, referred to as D-alanine, by the action of a catalytic enzyme. In addition to being an isomerase, mutarotase is responsible for catalysing the conversion of a-D-glucose to B-D-glucose. Ligase is one of 50 enzymes that are engaged in catalysing processes that are involved in the conversion of one kind of energy to another.

Types

• Triose Phosphate

It is a kind of phosphate. Three-phosphate isomerase is regarded to be an enzyme that catalyses the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate, which occurs in the presence of dihydroxyacetone phosphate. Triose Phosphate Isomerase is a critical enzyme in glycolysis, and it is essential for the production of energy at a high rate. When scientists began looking for TPI, they discovered that it could be found in practically every organism, including animals such as mammals and insects, as well as plants, fungi, and bacteria, among other things. However, there were other bacteria, such as ureaplasmas, that did not appear to have TPI since they did not execute glycolysis.

• Glucose Isomerase

It is a type of enzyme that breaks down glucose. In addition to fructose and xylose, glucose isomerase also can catalyse the reversible isomerisation of glucose into fructose and xylulose. High fructose corn syrup is produced in large quantities in the industrial manufacture of this enzyme, which is regarded to be necessary (HFCS). Despite their association with the food business, they are also beneficial and play a significant part in the production of biofuel.

• Phosphohexose Isomerase 

It is a kind of enzyme. A protein known as phosphohexose isomerase, also known as glucose phosphate isomerase, is believed to be present in the human body and is encoded by the GPI gene on chromosome 19. The GPI gene is located on chromosome 19 and is responsible for encoding the enzyme. Glucose phosphate isomerase protein is encoded by this gene, which belongs to the glucose phosphate isomerase family of proteins. The protein that appears to be encoded has been identified as a moonlighting protein, which is distinguished by its ability to perform mechanistically unique roles in different contexts. Specifically, the encoded protein, which is also known as neuroleukin, can operate as a neurotrophic factor, which is responsible for encouraging the survival of skeletal motor neurons as well as sensory neurons when it is found outside the cell.

As a result of its additional functions being a tumor-secreted cytokine and an angiogenic factor, the encoded protein is referred to as an autocrine motility factor (AMF).

• Peptidyl Prolyl Isomerase

It is an enzyme that helps to make peptidyl-prolyl isomerase. A type of enzyme that may be found in both prokaryotes and eukaryotes, Peptidyl Prolyl Isomerase is responsible for the interconversion of the cis and trans isomers of peptide bonds, along with the amino acid proline, in the presence of other enzymes. As previously stated, proline is known to have a particularly conformationally restricted peptide bond, which exists as a result of the cyclic structure of the amino acid, with its side chain attached to the secondary amine nitrogen of the amino acid. Because of steric hindrance, most amino acids are thought to have a strong, energetic preference, which aids in the support of the trans peptide bond conformation. However, the unusual structure of the proline is thought to be responsible for stabilizing the trans peptide bond conformation, which allows both isomers to be populated under biologically relevant conditions. Prolyl isomerase activity is found in several proteins, including cyclophilin, FKBPs, and parvulin. According to much research, it has been demonstrated that bigger proteins have an increased likelihood of possessing prolyl isomerase domains.

When compared to other natural amino acids, proline is believed to be one of the most distinctive since it has a relatively modest difference in free energy between the cis configuration of their peptide bond and the transform configuration, which is considered to be more prevalent.

• Isomerase for enoyl CoA

One type of enzyme, enoyl CoA isomerase, is responsible for catalysing the conversion of cis- or trans double bonds of coenzyme A (CoA) bound fatty acids, which are located at the gamma-carbon, into trans double bonds, which are present at the beta-carbon. The enzyme is essential in the metabolism of unsaturated fatty acids during beta-oxidation, and it is also involved in the metabolism of saturated fatty acids.

Because of its involvement in beta-oxidation, which is considered to be one of the most frequently used pathways for fatty acid degradation of unsaturated fatty acids, Enoyl CoA isomerase, as well as double bonds, which are present at add-numbered carbon positions, is evident from the preceding paragraph. To carry out this procedure, they begin by shifting the double bond position in the acyl-CoA intermediates and attempting to convert them to 3-cis or trans-enoyl-CoA and 2-trans-enoyl-CoA, respectively.

Conclusion

In this article, we addressed various key enzymes, some of which are found in the human body and some of which are not, but the vast majority of which are found in every living organism on the planet. These enzymes are found in nature and assist in the smooth execution of a wide range of functions. They play an important part in a variety of processes.