lactonizing enzyme from Asp to Asn or from Glu to Gln is that it can help to understand the effect of the metal ligand on the catalytic process and the binding site. Comparison between Muconate Lactonizing Enzymes and Mandelate Racemase Mandelate Racemase has a strong relationship to Muconate Lactonizing Enzymes. Even though Muconate lactonizing enzyme and Mandelate Racemase catalyse different chemical reactions that is required by Pseudomonas putida for the catabolic processes, they are structurally very similar to one another. According to the Nature International Journal of Science, both the enzymes are "26% identical in their primary structure." Based on the Nature International Journal of Science, this characteristic of homologous structure is said to have been evolved from a common ancestor. This feature helps in modifying the enzymatic activities for the metabolic pathways. According to the book, Enzymatic Mechanism, by Perry A. Frey and Dexter B. Northrop, Muconate lactonizing enzymes and Mandelate Racemase are both the member of enolase superfamily. Even though both the enzyme are different in their chemical reactions, they both have the same end product that leads to extracting a proton from an alpha carbon to a carboxylate ion. One of the advantage of the similarities between the structure of these two enzymes is to generate a high quality structural alignment that can help to improve their composition and strengthen the rate of reaction. The following table helps to identify some of the similarities between both the enzymes :- While the similarities are very prevalent, the difference between these two enzymes serve to understand the differences in the packaging of the enzyme in the crystal form. The following table helps to identify some of the differences between both the enzymes :- References External links EC 5.5.1