Disease relevance of prephenate

• Comparison of the deduced amino acid sequence of pheC from P. aeruginosa with those of the prephenate dehydratases of Corynebacterium glutamicum, Bacillus subtilis, E. coli, and Pseudomonas stutzeri by standard pairwise alignments did not establish obvious homology [1].
• Prephenate dehydratase from Bacillus subtilis was found to exist in three states of aggregation [2].
• Dual biosynthetic pathways diverge from prephenate to L-tyrosine in Pseudomonas aeruginosa, with 4-hydroxyphenylpyruvate and L-arogenate being the unique intermediates of these pathways [3].
• A reaction sequence is proposed for the conversion of prephenate to DHPA, involving an allylic rearrangement, followed by 1,4 reduction of the resulting conjugated diene and a combined decarboxylation/dehydration [4].
• Enzymes of tyrosine biosynthesis (prephenate dehydrogenase and arogenate dehydrogenase) were characterized in 90 species currently classified within the genera Pseudomonas, Xanthomonas, and Alcaligenes [5].

High impact information on prephenate

• Interactions and the mechanism of catalysis of chorismate --> prephenate by the EcCM enzyme are discussed [6].
• Chorismate mutase acts at the first branch-point of aromatic amino acid biosynthesis and catalyzes the conversion of chorismate to prephenate [7].
• Chorismate mutase (EC 5.4.99.5) catalyzes the intramolecular rearrangement of chorismate to prephenate [8].
• The enzyme prephenate dehydrogenase catalyzes the oxidative decarboxylation of prephenate to 4-hydroxyphenylpyruvate for the biosynthesis of tyrosine [9].
• The new metabolite is even more acid labile than is prephenate and is quantitatively converted to phenyllactate at mildly acidic pH [10].

Chemical compound and disease context of prephenate

• The prephenate dehydrogenase activity of the bifunctional enzyme chorismate mutase-prephenate dehydrogenase from Escherichia coli catalyzes the oxidative decarboxylation of both prephenate and deoxoprephenate, which lacks the keto group in the side chain (V 78% and V/K 18% those of prephenate) [11].
• X. campestris is like P. aeruginosa (and unlike E. coli) in its possession of dual flow routes to both L-phenylalanine and L-tyrosine from prephenate [12].
• Chorismate mutase/prephenate dehydrogenase from Escherichia coli K12: purification, characterization, and identification of a reactive cysteine [13].
• Second, the regulatory domain of the Buchnera prephenate dehydratase shows changes in the ESRP sequence, which is involved in the allosteric binding of phenylalanine and is strongly conserved in prephenate dehydratase proteins from practically all known organisms [14].
• The prephenate dehydrogenase component of the bifunctional T-protein in enteric bacteria can utilize L-arogenate [15].

Biological context of prephenate

• The active sites of all three of these structures are very similar and provide a structural basis for the biochemical studies that indicate a pericyclic mechanism for conversion of chorismate to prephenate [16].
• Recently, the sequencing of the chloroeremomycin gene cluster from Amycolatopsis orientalis gave new insights into the biosynthetic pathway and allowed for the prediction of a four enzyme pathway leading to L-p-hydroxyphenylglycine from the common metabolite prephenate [17].
• The phe operon consists of promoter, operator, leader region containing the phe attenuator and the pheA gene encoding chorismate mutase/prephenate dehydratase [18].
• As expected of a common catalytic site, dehydrogenase activity with either prephenate or L-arogenate was highly sensitive to inhibition by L-tyrosine [15].
• Molecular cloning with a pMEA300-derived shuttle vector and characterization of the Amycolatopsis methanolica prephenate dehydratase gene [19].

Anatomical context of prephenate

• A prephenate aminotransferase enzyme that produces L-arogenate was demonstrated in extracts from cultured-cell populations of Nicotiana silvestris [20].
• The substrate saturation curve of the complexed prephenate dehydratase I was sigmoid; a Km value of 0.18 mM was calculated for prephenate [21].

Associations of prephenate with other chemical compounds

• Co-accumulation of prephenate, L-arogenate, and spiro-arogenate in a mutant of Neurospora [22].
• The pH dependencies of log (V/KprephenateEt) and of pKi for hydroxyphenyllactate show that the wild-type dehydrogenase possesses a group with a pK of 8.8 that must be protonated for binding prephenate to the enzyme [23].
• The effects of phenylalanine, NaCl and pH on the conformation of chorismate mutase/prephenate dehydratase have been investigated, using measurements of far and near-ultraviolet circular dichroic spectra and ultraviolet difference spectra [24].
• Chorismate mutase/prephenate dehydrogenase: protection of the active site(s) against inactivation by iodoacetamide [proceedings] [25].
• These results are interpreted as indicating that both of these cysteine residues are at, or near to, the prephenate dehydratase active site and are possibly essential for the prephenate dehydratase activity of the enzyme [26].

Gene context of prephenate

• These libraries were placed under selection in lacZ or pheA deficient strains of E. coli to investigate whether they sample sufficient diversity to contain mutants with acquired beta-galactosidase or prephenate dehydratase activities [27].
• Characterization of the prephenate dehydrogenase-encoding gene, TYR1, from Saccharomyces cerevisiae [28].
• The activity of tas complements the prephenate dehydrogenase dysfunction of tyrA14 (the chorismate mutase activity of tyrA possibly being still functional) [29].
• As one example of advantageous biochemical potential, the presence of CM-F in Salmonella typhimurium increases the capacity for prephenate accumulation in a tyrA auxotroph [30].
• L-serine did not inhibit in vitro prephenate dehydratase activity, and the expression of pheA, which encodes the prephenate dehydratase, was not depressed by L-serine [31].

Analytical, diagnostic and therapeutic context of prephenate

• Probing the catalytic mechanism of prephenate dehydratase by site-directed mutagenesis of the Escherichia coli P-protein dehydratase domain [32].
• The Fourier transform infrared (FTIR) spectrum of the complex between prephenate and the monofunctional chorismate mutase from Bacillus subtilis displays one prominent band at 1714 cm-1 [33].
• As a preliminary to sequence analysis, a small DNA insertion at codon 338 of the pheA gene unexpectedly resulted in a partial loss of prephenate dehydratase feedback inhibition [34].
• Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris [20].
• A new simplified procedure for the purification of chorismate mutase/prephenate dehydratase, based on affinity chromatography on Sepharosyl-phenylalanine, has been developed [35].

References