Regulation of prephenate dehydratase in coryneform species of bacteria by l-phenylalanine and by remote effectors

Fazel, Akram M.; Jensen, Roy A.

doi:10.1016/0003-9861(80)90343-4

Cited by 26 publications

(17 citation statements)

References 25 publications

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“…However, a less straightforward (albeit rather common) pattern for the biosynthesis of L-phenylalanine and L-tyrosine in nature is the utilization of L-arogenate for L-tyrosine synthesis but not for L-phenylalanine synthesis. This occurs in cyanobacteria (69), coryneform bacteria (24)(25)(26), and other actinomycetes such as Amycolatopsis methanolica (1). In fact, in the absence of early information that L-arogenate could be a precursor of phenylalanine, L-arogenate was initially named "pretyrosine" (69).…”

Section: Tyra and L-tyrosine Biosynthesis Enzyme Order Alternatives Dmentioning

confidence: 99%

Cohesion Group Approach for Evolutionary Analysis of TyrA, a Protein Family with Wide-Ranging Substrate Specificities

Bonner

Disz

Hwang

et al. 2008

Microbiol Mol Biol Rev

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SUMMARY Many enzymes and other proteins are difficult subjects for bioinformatic analysis because they exhibit variant catalytic, structural, regulatory, and fusion mode features within a protein family whose sequences are not highly conserved. However, such features reflect dynamic and interesting scenarios of evolutionary importance. The value of experimental data obtained from individual organisms is instantly magnified to the extent that given features of the experimental organism can be projected upon related organisms. But how can one decide how far along the similarity scale it is reasonable to go before such inferences become doubtful? How can a credible picture of evolutionary events be deduced within the vertical trace of inheritance in combination with intervening events of lateral gene transfer (LGT)? We present a comprehensive analysis of a dehydrogenase protein family (TyrA) as a prototype example of how these goals can be accomplished through the use of cohesion group analysis. With this approach, the full collection of homologs is sorted into groups by a method that eliminates bias caused by an uneven representation of sequences from organisms whose phylogenetic spacing is not optimal. Each sufficiently populated cohesion group is phylogenetically coherent and defined by an overall congruence with a distinct section of the 16S rRNA gene tree. Exceptions that occasionally are found implicate a clearly defined LGT scenario whereby the recipient lineage is apparent and the donor lineage of the gene transferred is localized to those organisms that define the cohesion group. Systematic procedures to manage and organize otherwise overwhelming amounts of data are demonstrated.

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Section: Tyra and L-tyrosine Biosynthesis Enzyme Order Alternatives Dmentioning

confidence: 99%

Cohesion Group Approach for Evolutionary Analysis of TyrA, a Protein Family with Wide-Ranging Substrate Specificities

Bonner

Disz

Hwang

et al. 2008

Microbiol Mol Biol Rev

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“…Due to the importance of Corynebacterium glutamicum in the industrial production of amino acids (27), the enzymology of aromatic amino acid biosynthesis in this gram-positive organism has been extensively investigated (7,8,14,15). While several overproducing variants have been isolated, the previous lack of gene transfer mechanisms limited the characterization of these regulatory mutants to biochemical assessments of their phenotypic response.…”

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confidence: 99%

Molecular cloning and nucleotide sequence of the Corynebacterium glutamicum pheA gene

Follettie¹,

Sinskey²

1986

J Bacteriol

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The pheA gene of Corynebacterium glutamicum encoding prephenate dehydratase was isolated from a gene bank constructed in C. glutamicum. The specffic activity of prephenate dehydratase was increased six-fold in strains harboring the cloned gene. Genetic and strucetural evidence is presented which indicates that prephenate dehydratase and chorismate mutase were catalyzed by-separate enzymes in this species. The C. glutamicum pheA gene, subcloned in both orientations with respect to the Escherichia coli vector pUC8, was able to complement an E. coli pheA auxotroph. The nucleotide sequence of the C. glutamicum pheA gene predicts a 315-residue protein product with a molecular weight of 33,740. The deduced protein product demonstrated sequence homology to the C-terminal two-thirds of the bifunctional E. coli enzyme chorismate mutase-P-prephenate dehydratase.

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“…Determination of the possible sensitivity of arogenate dehydratase to feedback inhibition by L-phenylalanine is technically difficult since the assay involves measurement of phenylalanine product formed. In several systems prephenate dehydratase activity is stabilized or activated, or both, by L-leucine, L-methionine, or L-tyrosine (13,29,30 (iii) DAHP synthase. In crude extracts the activity of DAHP synthase deviated from proportionality rather dramatically at higher protein concentrations (Fig.…”

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confidence: 99%

“…In addition, a large number of Pseudomonas and Alcaligenes species have been shown to possess dual pathways to L-tyrosine (8,27). For L-phenylalanine biosynthesis the most common pathway appears to be the traditional phenylpyruvate route (13,16,20,22). In Pseudomonas aeruginosa enzymes of both the phenylpyruvate route and the alternative arogenate route have been characterized (27,28 (25).…”

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The aromatic amino acid pathway branches at L-arogenate in Euglena gracilis.

Byng¹,

Whitaker²,

Shapiro³

et al. 1981

Mol. Cell. Biol.

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The recently characterized amino acid L-arogenate (Zamir et al., J. Am. Chem. Soc. 102:4499-4504, 1980) may be a precursor of either L-phenylalanine or Ltyrosine in nature. Euglena gracilis is the first example of an organism that uses L-arogenate as the sole precursor of both L-tyrosine and L-phenylalanine, thereby creating a pathway in which L-arogenate rather than prephenate becomes the metabolic branch point. E. gracilis ATCC 12796 was cultured in the light under myxotrophic conditions and harvested in late exponential phase before extract preparation for enzymological assays. Arogenate dehydrogenase was dependent upon nicotinamide adenine dinucleotide phosphate for activity. L-Tyrosine inhibited activity effectively with kinetics that were competitive with respect to Larogenate and noncompetitive with respect to nicotinamide adenine dinucleotide phosphate. The possible inhibition of arogenate dehydratase by L-phenylalanine has not yet been determined. Beyond the latter uncertainty, the overall regulation of aromatic biosynthesis was studied through the characterization of 3-deoxy-Darabino-heptulosonate 7-phosphate synthase and chorismate mutase. 3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase was subject to noncompetitive inhibition by L-tyrosine with respect to either of the two substrates. Chorismate mutase was feedback inhibited with equal effectiveness by either L-tyrosine or Lphenylalanine. L-Tryptophan activated activity of chorismate mutase, a pHdependent effect in which increased activation was dramatic above pH 7.8. LArogenate did not affect activity of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase or of chorismate mutase. Four species of prephenate aminotransferase activity were separated after ion-exchange chromatography. One aminotransferase exhibited a narrow range of substrate specificity, recognizing only the combination of L-glutamate with prephenate, phenylpyruvate, or 4-hydroxyphenylpyruvate. Possible natural relationships between Euglena spp. and fungi previously considered in the literature are discussed in terms of data currently available to define enzymological variation in the shikimate pathway.

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Regulation of prephenate dehydratase in coryneform species of bacteria by l-phenylalanine and by remote effectors

Cited by 26 publications

References 25 publications

Cohesion Group Approach for Evolutionary Analysis of TyrA, a Protein Family with Wide-Ranging Substrate Specificities

Cohesion Group Approach for Evolutionary Analysis of TyrA, a Protein Family with Wide-Ranging Substrate Specificities

Molecular cloning and nucleotide sequence of the Corynebacterium glutamicum pheA gene

The aromatic amino acid pathway branches at L-arogenate in Euglena gracilis.

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