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  • 1
    Electronic Resource
    Electronic Resource
    The evolutionary pattern of aromatic amino acid biosynthesis and the emerging phylogeny of pseudomonad bacteria (1983)
    Springer
    Journal of molecular evolution 19 (1983), S. 272-282 
    Details
    ISSN: 1432-1432
    Keywords: Microbial phylogeny ; Evolution ; Aromatic biosynthesis ; Regulatory enzymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pseudomonad bacterial are a phylogenetically diverse assemblage of species named within contemporary genera that includePseudomonas, Xanthomonas andAlcaligenes. Thus far, five distinct rRNA homology groups (Groups I through V) have been established by oligonucleotide cataloging and by rRNA/DNA hybridization. A pattern of enzymic features of aromatic amino acid biosynthesis (enzymological patterning) is conserved at the level of rRNA homology, five distinct and unambiguous patterns therefore existing in correspondence with the rRNA homology groups. We sorted 87 pseudomonad strains into Groups (and Subgroups) by aromatic pathway patterning. The reliability of this methodology was tested in a blind study using coded cultures of diverse pseudomonad organisms provided by American Type Culture Collection. Fourteen of 14 correct assignments were made at the Group level (the level of rRNA homology), and 12 of 14 correct assignments were made at the finer-tuned Subgroup levels. Many strains of unknown rRNA-homology affiliation had been placed into tentative rRNA groupings based upon enzymological patterning. Positive confirmation of such strains as members of the predicted rRNA homology groups was demonstrated by DNA/rRNA hybridization in nearly every case. It seems clear that the combination of these molecular approaches will make it feasible to deduce the evolution of biochemical-pathway construction and regulation in parallel with the emerging phylogenies of microbes housing these pathways.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02099974
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  • 2
    Electronic Resource
    Electronic Resource
    The recent evolutionary origin of the phenylalanine-sensitive isozyme of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase in the enteric lineage of bacteria (1987)
    Springer
    Journal of molecular evolution 25 (1987), S. 159-167 
    Details
    ISSN: 1432-1432
    Keywords: Metabolic evolution ; Aromatic biosynthesis ; Regulatory isozymes ; Enteric bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Evolutionary events that generated the three regulatory isozymes of 3-deoxy-d-arabino-heptulosonate 7-phosphate (DAHP) synthase present in contemporary strains ofEscherichia coli have been proposed recently [Ahmad et al. (1986) J Bacteriol 165:146–154]. The phylogenetic subdivision of gram-negative prokaryotes studied (Superfamily B) includes enteric bacteria, anOceanospirillum cluster, pseudomonad Group I (e.g.,Pseudomonas aeruginosa), pseudomonad Group V (e.g.,Xanthomonas), and theAcinetobacter grouping. DAHP synthase-phe, a regulatory isozyme subject to allosteric control byl-phenylalanine, was the last member of the isozyme family to evolve. Thus, DAHP synthase-phe is absent throughout Superfamily B except within the enteric lineage. Bacteria that make up the enteric lineage (Escherichia, Klebsiella, Erwinia, Serratia, Proteus, Aeromonas, andAlteromonas) were examined in detail; DAHP synthasephe was present in each of these organisms. Therefore, the isozyme originated between the separation of the enteric andOceanospirillum lineages, prior to the divergence ofAlteromonas putrefaciens (44% homology withE. coli by DNA:rRNA hybridization) from the rest of the enteric lineage. DAHP synthase-tyr and DAHP synthase-trp were uniformly present within the enteric lineage, although it was often necessary to derepress DAHP synthase-trp by physiological manipulation in order to demonstrate its presence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02101758
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  • 3
    Electronic Resource
    Electronic Resource
    Phenylalanine hydroxylase and isozymes of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in relationship to the phylogenetic position of Pseudomonas acidovorans (Ps. sp. ATCC 11299a) (1985)
    Springer
    Archives of microbiology 141 (1985), S. 32-39 
    Details
    ISSN: 1432-072X
    Keywords: Phylogeny ; Pseudomonads ; Aromatic biosynthesis ; DAHP synthase ; Phenylalanine hydroxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The evolution of aromatic amino acid biosynthesis and its regulation is under study in a large assemblage of prokaryotes (Superfamily A) whose phylogenetic arrangement has been constructed on the criterion of oligonucleotide cataloging. One section of this Superfamily consists of a well defined (rRNA homology) cluster denoted as Group III pseudomonads. Pseudomonas acidovorans ATCC 11299a, a Group III member, was chosen for indepth studies of 3-deoxy-d-arabino-heptulosonate 7-phosphate (DAHP) synthase, the initial regulatory enzyme of aromatic biosynthesis. This strain is of particular interest for evolutionary studies of aromatic metabolism because it possesses phenylalanine hydroxylase, an enzyme whose physiological role and distribution among prokaryotes is largely unknown. Although P. acidovorans ATCC 11299a has been of uncertain identity, we now establish it unambiguously as a species of acidovorans by virtue of its 87% DNA homology with P. acidovorans ATCC 15668 (type strain). This result conformed with enzyme patterning studies which placed ATCC 11299a into pseudomonad Group IIIa, a subgroup containing the acidovorans species. Crude extracts of Group III pseudomonads had previously been shown to share, as a common group characteristic, sensitivity of DAHP synthase to feedback inhibition by either l-tyrosine or l-phenylalanine. Detailed studies with partially purified preparations from strain ATCC 11299a revealed the presence of two distinct regulatory isozymes, DAHP synthase-phe and DAHP synthase-tyr. DAHP synthase-tyr is tightly controlled by l-tyrosine with 50% inhibition of activity being achieved at 4.0 μM effector. DAHP synthase-phe is inhibited 50% by 40 μM l-phenylalanine and exhibits dramatic changes in levels of activity, as well as chromatographic elution patterns, in response to dithiothreitol. This two-isozyme pattern of DAHP synthase has not been described previously, although it may prove to be widespread.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446736
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    Paper (German National Licenses)
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