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The shikimate pathway (shikimic acid pathway) is a seven-step metabolic pathway used by bacteria, archaea, fungi, algae, some protozoans, and plants for the biosynthesis of folates and aromatic amino acids (tryptophan, phenylalanine, and tyrosine). This pathway is not found in mammals.
The Shikimate pathway has become a focus of research into the development of herbicides and antimicrobial agents because it is an essential pathway in many plants, bacteria, and parasites but does not exist in mammals. [1] Inhibitors of the shikimate pathway in mycobacterium have the potential of treating tuberculosis. [5] [6]
The shikimate pathway, named after shikimic acid as important intermediate, is a seven-step metabolic route used by bacteria, fungi, algae, parasites, and plants for the biosynthesis of aromatic amino acids (phenylalanine, tyrosine, and tryptophan).
3-Dehydroquinate synthase catalyzes the second step in the shikimate pathway, which is essential for the production of aromatic amino acids in bacteria, plants, and fungi, but not mammals. This makes it an ideal target for new antimicrobial agents, anti-parasitic agents, and herbicides. [ 1 ]
EPSP synthase catalyzes the reaction which converts shikimate-3-phosphate plus phosphoenolpyruvate to 5-enolpyruvylshikimate-3-phosphate (EPSP) by way of an acetal-like tetrahedral intermediate. [ 9 ] [ 10 ] Basic and acidic amino acids in the active site are involved in deprotonation of the hydroxyl group of PEP and in the proton-exchange ...
DAHP synthase is the first enzyme that acts in the Shikimate Pathway in microorganisms, fungi, and plants. A series of catalytic mechanisms result in the production of aromatic amino acids required for metabolism. However, another biological function of the enzyme is to regulate the amount of carbon that enters the shikimate pathway.
Shikimate kinase (EC 2.7.1.71) is an enzyme that catalyzes the ATP-dependent phosphorylation of shikimate to form shikimate 3-phosphate. [1] This reaction is the fifth step of the shikimate pathway, [2] which is used by plants and bacteria to synthesize the common precursor of aromatic amino acids and secondary metabolites.
In enzymology, chorismate mutase (EC 5.4.99.5) is an enzyme that catalyzes the chemical reaction for the conversion of chorismate to prephenate in the pathway to the production of phenylalanine and tyrosine, also known as the shikimate pathway. Hence, this enzyme has one substrate, chorismate, and one product, prephenate. Chorismate mutase is ...