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. 1981 Aug;147(2):526–534. doi: 10.1128/jb.147.2.526-534.1981

Diverse Enzymological Patterns of Phenylalanine Biosynthesis in Pseudomonads Are Conserved in Parallel with Deoxyribonucleic Acid Homology Groupings

Robert J Whitaker 1, Graham S Byng 1, Robert L Gherna 2, R A Jensen 1
PMCID: PMC216073  PMID: 7263614

Abstract

l-Tyrosine biosynthesis in nature has proven to be an exceedingly diverse gestalt of variable biochemical routing, cofactor specificity of pathway dehydrogenases, and regulation. A detailed analysis of this enzymological patterning of l-tyrosine biosynthesis formed a basis for the clean separation of five taxa among species currently named Pseudomonas, Xanthomonas, or Alcaligenes (Byng et al., J. Bacteriol. 144:247-257, 1980). These groupings paralleled taxa established independently by ribosomal ribonucleic acid/deoxyribonucleic acid (DNA) homology relationships. It was later found that the distinctive allosteric control of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase in group V, a group dominated by most named species of Xanthomonas (Whitaker et al., J. Bacteriol. 145:752-759, 1981), was the most striking and convenient criterion of group V identity. Diversity in the biochemical routing of l-phenylalanine biosynthesis and regulation was also found, and phenylalanine patterning is in fact the best single enzymatic indicator of group IV (Pseudomonas diminuta and Pseudomonas vesicularis) identity. Enzymological patterning of l-phenylalanine biosynthesis allowed discrimination of still finer groupings consistently paralleling that achieved by the criterion of DNA/DNA hybridization. Accordingly, the five ribosomal ribonucleic acid/DNA homology groups further separate into eight DNA homology subgroups and into nine subgroups based upon phenylalanine pathway enzyme profiling. (Although both fluorescent and nonfluorescent species of group I pseudomonads fall into a common DNA homology group, fluorescent species were distinct from nonfluorescent species in our analysis.) Hence, phenylalanine patterning data provide a relatively fine-tuned probe of hierarchical level. The combined application of these various enzymological characterizations, feasibly carried out in crude extracts, offers a comprehensive and reliable definition of 11 pseudomonad subgroups, 2 of them being represented by species of Alcaligenes.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ballard R. W., Doudoroff M., Stanier R. Y., Mandel M. Taxonomy of the aerobic psuedomonads: Pseudomonas diminuta and P. vesiculare. J Gen Microbiol. 1968 Oct;53(3):349–361. doi: 10.1099/00221287-53-3-349. [DOI] [PubMed] [Google Scholar]
  2. Ballard R. W., Palleroni N. J., Doudoroff M., Stanier R. Y., Mandel M. Taxonomy of the aerobic pseudomonads: Pseudomonas cepacia, P. marginata, P. alliicola and P. caryophylli. J Gen Microbiol. 1970 Feb;60(2):199–214. doi: 10.1099/00221287-60-2-199. [DOI] [PubMed] [Google Scholar]
  3. Baptist J. N., Shaw C. R., Mandel M. Comparative zone electrophoresis of enzymes of Pseudomonas solanacearum and Pseudomonas cepacia. J Bacteriol. 1971 Nov;108(2):799–803. doi: 10.1128/jb.108.2.799-803.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Baumann L., Baumann P. Studies of relationship among terrestrial Pseudomonas, Alcaligenes, and enterobacteria by an immunological comparison of glutamine synthetase. Arch Microbiol. 1978 Oct 4;119(1):25–30. doi: 10.1007/BF00407923. [DOI] [PubMed] [Google Scholar]
  5. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  6. Byng G. S., Whitaker R. J., Gherna R. L., Jensen R. A. Variable enzymological patterning in tyrosine biosynthesis as a means of determining natural relatedness among the Pseudomonadaceae. J Bacteriol. 1980 Oct;144(1):247–257. doi: 10.1128/jb.144.1.247-257.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Byng G. S., Whitaker R. J., Shapiro C. L., Jensen R. A. The aromatic amino acid pathway branches at L-arogenate in Euglena gracilis. Mol Cell Biol. 1981 May;1(5):426–438. doi: 10.1128/mcb.1.5.426. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Calhoun D. H., Pierson D. L., Jensen R. A. Channel-shuttle mechanism for the regulation of phenylalanine and tyrosine synthesis at a metabolic branch point in Pseudomonas aeruginosa. J Bacteriol. 1973 Jan;113(1):241–251. doi: 10.1128/jb.113.1.241-251.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Fazel A. M., Bowen J. R., Jensen R. A. Arogenate (pretyrosine) is an obligatory intermediate of L-tyrosine biosynthesis: confirmation in a microbial mutant. Proc Natl Acad Sci U S A. 1980 Mar;77(3):1270–1273. doi: 10.1073/pnas.77.3.1270. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. HOLLOWAY B. W. Genetic recombination in Pseudomonas aeruginosa. J Gen Microbiol. 1955 Dec;13(3):572–581. doi: 10.1099/00221287-13-3-572. [DOI] [PubMed] [Google Scholar]
  11. Jensen R. A., Calhoun D. H., Stenmark S. L. Allosteric inhibition of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase by tyrosine, tryptophan and phenylpyruvate in Pseudomonas aeruginosa. Biochim Biophys Acta. 1973 Jan 12;293(1):256–268. doi: 10.1016/0005-2744(73)90398-7. [DOI] [PubMed] [Google Scholar]
  12. Jensen R. A., Nasser D. S., Nester E. W. Comparative control of a branch-point enzyme in microorganisms. J Bacteriol. 1967 Nov;94(5):1582–1593. doi: 10.1128/jb.94.5.1582-1593.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Jensen R. A., Pierson D. L. Evolutionary implications of different types of microbial enzymology for L-tyrosine biosynthesis. Nature. 1975 Apr 24;254(5502):667–671. doi: 10.1038/254667a0. [DOI] [PubMed] [Google Scholar]
  14. Jensen R. A., Stenmark S. L. Comparative allostery of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthetase as a molecular basis for classification. J Bacteriol. 1970 Mar;101(3):763–769. doi: 10.1128/jb.101.3.763-769.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Jensen R. A., Zamir L., Saint Pierre M., Patel N., Pierson D. L. Isolation and preparation of pretyrosine, accumulated as a dead-end metabolite by Neurospora crassa. J Bacteriol. 1977 Dec;132(3):896–903. doi: 10.1128/jb.132.3.896-903.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. LéJohn H. B. Enzyme regulation, lysine pathways and cell wall structures as indicators of major lines of evolution in fungi. Nature. 1971 May 21;231(5299):164–168. doi: 10.1038/231164a0. [DOI] [PubMed] [Google Scholar]
  17. Palleroni N. J., Ballard R. W., Ralston E., Doudoroff M. Deoxyribonucleic acid homologies among some Pseudomonas species. J Bacteriol. 1972 Apr;110(1):1–11. doi: 10.1128/jb.110.1.1-11.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Palleroni N. J., Doudoroff M. Phenotypic characterization and deoxyribonucleic acid homologies of Pseudomonas solanacearum. J Bacteriol. 1971 Sep;107(3):690–696. doi: 10.1128/jb.107.3.690-696.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Palleroni N. J., Doudoroff M., Stanier R. Y., Solánes R. E., Mandel M. Taxonomy of the aerobic pseudomonads: the properties of the Pseudomonas stutzeri group. J Gen Microbiol. 1970 Feb;60(2):215–231. doi: 10.1099/00221287-60-2-215. [DOI] [PubMed] [Google Scholar]
  20. Patel N., Pierson D. L., Jensen R. A. Dual enzymatic routes to L-tyrosine and L-phenylalanine via pretyrosine in Pseudomonas aeruginosa. J Biol Chem. 1977 Aug 25;252(16):5839–5846. [PubMed] [Google Scholar]
  21. Patel N., Stenmark-Cox S. L., Jensen R. A. Enzymological basis of reluctant auxotrophy for phenylalanine and tyrosine in Pseudomonas aeruginosa. J Biol Chem. 1978 May 10;253(9):2972–2978. [PubMed] [Google Scholar]
  22. Ralston E., Palleroni N. J., Doudoroff M. Deoxyribonucleic acid homologies of some so-called "Hydrogenomonas" species. J Bacteriol. 1972 Jan;109(1):465–466. doi: 10.1128/jb.109.1.465-466.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Shapiro C. L., Jensen R. A., Wilson K. A., Bowen J. R. An assay for activity of arogenate dehydratase base upon the selective oxidation of arogenate. Anal Biochem. 1981 Jan 1;110(1):27–30. doi: 10.1016/0003-2697(81)90106-8. [DOI] [PubMed] [Google Scholar]
  24. Stanier R. Y., Palleroni N. J., Doudoroff M. The aerobic pseudomonads: a taxonomic study. J Gen Microbiol. 1966 May;43(2):159–271. doi: 10.1099/00221287-43-2-159. [DOI] [PubMed] [Google Scholar]
  25. Stenmark-Cox S., Jensen R. A. Prephenate dehydrogenase from Pseudomonas aeruginosa is a regulated component of the channel-shuttle mechanism controlling tyrosine-phenylalanine synthesis. Arch Biochem Biophys. 1975 Apr;167(2):540–546. doi: 10.1016/0003-9861(75)90497-x. [DOI] [PubMed] [Google Scholar]
  26. Stenmark S. L., Pierson D. L., Jensen R. A., Glover G. I. Blue-green bacteria synthesise L-tyrosine by the pretyrosine pathway. Nature. 1974 Feb 1;247(5439):290–292. doi: 10.1038/247290a0. [DOI] [PubMed] [Google Scholar]
  27. Whitaker R. J., Byng G. S., Gherna R. L., Jensen R. A. Comparative allostery of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase as an indicator of taxonomic relatedness in pseudomonad genera. J Bacteriol. 1981 Feb;145(2):752–759. doi: 10.1128/jb.145.2.752-759.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]

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