Biosynthesis phosphoenol pyruvate

The shikimate biosynthetic pathway occurs in bacteria, plants, and fungi (including yeasts) and is a major entry into the biosynthesis of primary and secondary metabolites, for example aromatic amino acids, menaquinones, vitamins, and antibiotics [1], Starting from erythrose-4-phosphate (E4P) and phosphoenol-pyruvate... 

Fig. 8.13 Biosynthesis of aromatic compounds in E. coli [71]. Compounds E4P, D-erythrose-4-phosphate PEP, phosphoenol-pyruvate DAHP, 3-deoxy-D-arab/> o-heptulo-...

Figure 7 Biosynthesis of aromatic amino acids and products derived from phenylalanine or from intermediates of the shikimate pathway. Biosynthetically equivalent positions are indicated by colored bars. The atoms indicated by the blue bars are equivalent to atoms from phosphoenol pyruvate precursor followed by the loss of one carbon atom by decarboxylation.

KDO synthetase catalyzes the reaction of arabinose 5-phosphate (29 Ara-5-P) and phosphoenol pyruvate (PEP) to form KDO-8-P (30 Scheme 9). KDO synthetase is not commercially available but has been isolated from E. coli and used in the synthesis of KDO-8-P (63% from Ara-5-P, 38 mmol). KDO-8-P is a key intermediate in the synthesis of the lipopolysaccharide region of Gram-negative bacteria (LPS). Inhibitors of LPS biosynthesis are targets for the design of antimicrobial drugs. ... 

The starting compounds for the biosynthesis of vanillic acid in genetically modified Escherichia coli are erythrose 4-phosphate and phosphoenol pyruvate. The erythrose is an intermediate product in carbohydrate metabolism (Calvin cycle, dark reaction of photosynthesis). [154, 155] Phosphoenol pyruvate is produced in several steps from 3-phosphoglyceric acid, or from a technical point of view, from succinic acid via the citric acid cycle. [156]... 

The biosynthesis of the aromatic amino acids proceeds via shikimic acid. [56] The starting point is erythrose-4-phosphate, which is produced in the Calvin cycle. The enzyme-catalysed aldol condensation with phosphoenol pyruvate leads to a heptulose, 3-deoxy-(D)-arahino-heptulonic add 7-phosphate. Elimination of phosphate produces an enol, which is converted hy a further aldol condensation into 3-dehydroquinic acid. Elimination of water and reduction then yield shikimic add. 

Besides the genes involved in biosynthesis of the PKS extender unit 106 and the PKS-NRPS machinery SalA-SalB, genes associated with the proposed biosynthesis of the novel nonproteinogenic amino acid 105 are present in the sal cluster. These include coding for a dedicated DAHP synthase sail which is thought to initiate the biosynthesis of amino acids through formation of 102 from phosphoenol pyruvate... 

For thermodynamic reasons, pyruvate-dependent aldolases have catabolic functions in vivo, whereas their counterparts employing (energy-rich) phosphoenol pyruvate as the donor are involved in the biosynthesis of keto-acids. However, both types of enzymes can be used to synthesize a-keto-p-hydroxy acids in vitro. 

Bacteria, fungi, and plants share a common pathway for the biosynthesis of aromatic amino acids with shikimic acid as a common intermediate and therefore named after it—the shikimate pathway. Availability of shikimic acid has proven to provide growth requirements to tryptophan, tyrosine, and phenylalanine triple auxotrophic bacterial strains. Chorismate is also the last common precursor in the aromatic amino acid biosynthetic pathway, but the pathway is not named after it, as it failed to provide growth requirements to the triple auxotrophs. The aromatic biosynthetic pathway starts with two molecules of phosphoenol pyruvate and one molecule of erythrose 4-phosphate and reach the common precursor, chorismate through shikimate. From chorismate, the pathway branches to form phenylalanine and tyrosine in one and tryptophan in another. Tryptophan biosynthesis proceeds from chorismate in five steps in all organisms. Phenylalanine and tyrosine can be produced by either or both of the two biosynthetic routes. So phenylalanine can be synthesized from arogenate or phenylpyruvate whereas tyrosine can be synthesized from arogenate or 4-hydroxy phenylpyruvate. 

The biosynthesis of the nucleoside skeleton of polyoxins has been studied using C- and C-labelled glucose, glycerate, and uridine substrates it was suggested that condensation of uridine as its 5 -aldehyde with phosphoenol pyruvate gives an octofuranuloseuronic acid nucleoside, which loses the two terminal carbon atoms by oxidative elimination followed by transamination to give the required uridyl-5-amino-5-deoxy-D-allofuranosyluronic acid structure. ... 

Phosphoenol pyruvate (55) and erythrose-4-phosphate (56) have been applied in biosynthesis of 3,4-dihydroxybenzoic acid (57) of the siderophore petrobactin, produced by B. anthracis str. Sterne (Scheme 18). ... 

In Tetrahymena pyriformis the radioactive carbon atom in phosphoenol [3- C]pyruvate is incorporated into the phosphonate carbon atom in 2-aminoethylphosphonic acid (46), confirming an earlier suggestion that an intramolecular rearrangement of PEP takes place during the biosynthesis of (46). The incorporation of label into (46) is inhibited to a greater extent by phosphonoacetaldehyde (47) than by 2-amino-3-phosphonopropionic acid (48) hence the latter may not be on the main... 

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