Shikimate kinase synthesis

In B. subtilis the single DAHPS enzyme is repressed most strongly by tyrosine, but maximal repression required the presence of both tyrosine and phenylalanine [121]. Tryptophan appeared to play no role in repression eontrol of synthesis of the enzyme. Nester et al. [121] also reported that a mixture of the three aromatic amino acids repressed synthesis of DAHPS, dehydroquinate synthetase, and shikimate kinase noncoordinately, but had no effect on the level of dehydroquinase. 

The synthesis of compound (44) as a potential transition-state analogue inhibitor of isochorismate synthase (IS) has been reported/ Compounds (45) and (46) have been synthesized from the known 6-fluoroshikimic acids (J. Chem. Soc., Chem. Commun., 1989, 1386) by treatment first with shikimate kinase then 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase and shown to be competitive inhibitors of chorismate synthase/ ... 

Phosphorylation of 3-hydroxyl group of shikimate by shikimate kinase (EC 2.7.1.71) with ATP as a cosubstrate initiates the biosynthesis pathway of anthranilic acid [2], This step also presents the first step of the shikimate pathway, which is a metabolic route used by bacteria, fungi, and plants for the biosynthesis of many aromatic products such as lignins, alkaloids, flavonoids, benzoic acid, and plant hormones, in addition to the aromatic amino acids (phenylalaiune, tyrosine, and tryptophan). The sequential EPSP synthesis is catalyzed by EPSP synthase (EC 2.5.1.19) through the addition of phosphoenolpyruvate to 3-phospho-shikimate followed elimination of phosphate. EPSP synthase belongs to the family of transferases, specifically to those transferring aryl... 

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