Disease relevance of pheA

• The structure also offers an explanation for its regulation by small ligands, such as tryptophan, a feature previously unknown in the prototypical Escherichia coli chorismate mutase [1].
• The 2.15 A crystal structure of Mycobacterium tuberculosis chorismate mutase reveals an unexpected gene duplication and suggests a role in host-pathogen interactions [1].
• Molecular cloning and nucleotide sequence of the Corynebacterium glutamicum pheA gene [2].
• The aroQ and pheA domains of the bifunctional P-protein from Xanthomonas campestris in a context of genomic comparison [3].
• Its tertiary and quaternary structures are related to that of Bacillus subtilis chorismate mutase, although their active sites are completely different [4].

High impact information on pheA

• Chorismate mutase (EC 5.4.99.5) catalyzes the intramolecular rearrangement of chorismate to prephenate [5].
• Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: the importance of electrostatic catalysis [5].
• Besides eliminating feedback inhibition, removal of the R-domain decreased the affinity of chorismate mutase for chorismate [6].
• Chorismate mutase catalyzes the first committed step toward the biosynthesis of the aromatic amino acids, phenylalanine and tyrosine [1].
• The gene Rv1885c from the genome of Mycobacterium tuberculosis H(37)R(v) encodes a monofunctional and secreted chorismate mutase (*MtCM) with a 33-amino-acid cleavable signal sequence; hence, it belongs to the *AroQ class of chorismate mutases [7].

Chemical compound and disease context of pheA

• Phenylalanine production by metabolically engineered Corynebacterium glutamicum with the pheA gene of Escherichia coli [8].
• The regulatory gene srlC controlling enzymes of sorbitol uptake and catabolism has been located on the E. coli genome as part of the linkage group cysI srlC attI86 pheA [9].
• The steady-state parameters kcat and kcat/Km for the monofunctional chorismate mutase from Bacillus subtilis (BsCM) decreased significantly with increasing concentrations of glycerol, whereas the 'sluggish' BsCM mutants C75A and C75S were insensitive to changes in microviscosity [10].
• Amino acid sequences of soluble tryptic peptides of chorismate mutase/prephenate dehydratase from Escherichia coli K12 [11].

Biological context of pheA

• The nucleotide sequence of the C. glutamicum pheA gene predicts a 315-residue protein product with a molecular weight of 33,740 [2].
• One of the seven rrn operons was found to be linked to pheA and another was found to be linked to aroE [12].
• The new selection system, in conjunction with combinatorial mutagenesis, renders the mechanism of the natural enzyme(s) accessible to further exploration and opens avenues for the improvement of first generation catalytic antibodies with chorismate mutase activity [5].

Associations of pheA with chemical compounds

• Moreover, the level of pheA expression was further elevated a fewfold when cells were starved of phenylalanine, suggesting that the attenuation regulation of pheA expression functions in heterogeneous C. glutamicum [8].
• 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 [13].

References