Substrate ambiguity of 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Neisseria gonorrhoeae in the context of its membership in a protein family containing a subset of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases

Journal of Bacteriology

Volumn 180, Issue 1, 1998, Pages 119-127

  Subramaniam, Prem S ^a   Xie, Gang ^a   Xia, Tianhui ^a   Jensen, Roy A ^a  

^a UNIVERSITY OF FLORIDA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 DEHYDRO 3 DEOXYPHOSPHOHEPTONATE ALDOLASE; 3 DEOXY MANNO OCTULOSONIC ACID; BACTERIAL ENZYME; PERIODATE; PHOSPHOENOLPYRUVATE; SYNTHETASE; THIOBARBITURIC ACID;

ALLOSTERISM; AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; NEISSERIA GONORRHOEAE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; NEISSERIA GONORRHOEAE; PROKARYOTA;

EID: 0031963257     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.1.119-127.1998     Document Type: Article

References (53)

1. Anderson, K. S., and K. A. Johnson. 1990. Kinetic and structural analysis of enzyme intermediates: lessons from EPSP synthase. Chem. Rev. 90:1131-1149.
2. Ballou, C. E. 1963. Preparation and properties of D-erythrose-4-phosphate. Methods Enzymol. 6:479-484.
3. Bentley, R. 1990. The shikimate pathway: a metabolic tree with many branches. Crit. Rev. Biochem. Mol. Biol. 5:307-384.
4. Bhatnagar, R. K., A. Berry, A. T. Hendry, and R. A. Jensen. 1989. The biochemical basis for growth inhibition by L-phenylalanine in Neisseria gonorrhoeae. Mol. Microbiol. 3:429-435.
5. Bolotin, A., V. Khazak, N. Stoynova, K. Ratmanova, Y. Yomantas, and Y. Kozlov. 1995. Identical amino acid sequence of the aroA(G) gene products of Bacillus subtilis 168 and B. subtilis Marburg strain. Microbiology 141:2219-2222.
6. Bonner, C. A., and R. A. Jensen, R. A. 1994. Cloning of cDNA encoding the bifunctional dehydroquinase • shikimate dehydrogenase of aromatic amino acid biosynthesis in Nicotiana tabacum. Biochem. J. 302:11-14.
7. Burrows, L. L., J. S. Lam, and R. Y. C. Lo. 1996. The kdsA gene of Pasteurella trehalosi (haemolytica) serotype T3 is functionally and genetically homologous to that of Escherichia coli. J. Endotoxin Res. 3:353-359.
8. Chang, H.-C., H. Maruyarna, R. S. Miller, and M. D. Lane. 1966. The enzymatic carboxylation of phosphoenolpyruvate. J. Biol. Chem. 241:2421-2430.
9. Chen, C., C. Liao, and W. Hsu. 1993. The cloning and nucleotide sequence of a Corynebacterium glutamicum 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase gene. FEMS Microbiol. Lett. 107:223-230.
10. Crawford, I. P. 1989. Evolution of a biosynthetic pathway: the tryptophan paradigm. Annu. Rev. Microbiol. 43:567-600.
11. Davies, W. D., and B. E. Davidson. 1982. The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase (phe) in Escherichia coli K-12. Nucleic Acids Res. 10:4045-4058.
12. DeLeo, A. B., J. Dayan, and D. B. Sprinson. 1973. Purification and kinetics of tyrosine-sensitive 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthetase from Salmonella. J. Biol. Chem. 248:2344-2353.
13. Doong, R. L., S. Ahmad, and R. A. Jensen. 1991. Higher plants express 3-deoxy-D-manno-octulosonate 8-phosphate synthase. Plant Cell Environ. 14:113-120.
14. Doong, R. L., J. E. Gander, R. J. Ganson, and R. A. Jensen. 1992. The cytosolic isoenzyme of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in Spinacia olearacea and other higher plants: extreme substrate ambiguity and other properties. Physiol. Plant 84:351-360.
15. Doong, R. L., and R. A. Jensen. 1992. Synonymy of the three apparent isoenzymes of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in Pisum sativum L. with 3-deoxy-D-manno-octulosonate 8-phosphate synthase and the DS/Co DS-Mn isoenzyme pair. New Phytol. 121:165-171.
16. Dotson, G. D., R. K. Dua, J. C. Clemens, E. W. Wooten, and R. W. Woodward. 1995. Overproduction and one-step purification of Escherichia coli 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase and oxygen transfer studies during catalysis using isotopic-shifted heteronuclear NMR. J. Biol. Chem. 270:13698-13705.
17. Fleischmann, R. D., M. D. Adams, O. White, R. A. Clayton, E. F. Kirkness, A. R. Keriavage, C. J. Bult, J.-F. Tomb, B. A. Dougherry, J. M. Merrick, K. McKenny, G. Sutton, W. FitzHug, C. Fields, J. D. Gocayne, J. Scott, R. Shirley, L.-L. Liu, A. Glodek, J. M. Kelley, J. F. Weidman, C. A. Phillips, T. Spriggs, E. Hedblom, M. D. Cotton, T. R. Utterback, M. C. Hanna, D. T. Nguyen, D. M. Saudek, R. C. Brandon, L. D. Fine, J. L. Fritchman, J. L. Fuhrmann, N. S. M. Geoghagen, C. L. Gnehm, L. A. McDonald, K. B. Small, C. M. Fraser, H. O. Smith, and J. C. Venter. 1995. Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269:496-512.
18. Floss, H. G., D. K. Onderka, and M. Carroll. 1972. Stereochemistry of the 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase reaction and the chorismate mutase reaction. J. Biol. Chem. 247:736-744.
19. Ganem, B. 1978. From glucose to aromatics: recent developments in natural products of the shikimic acid pathway. Tetrahedron 34:3353-3383.
20. Ganson, R. J., T. A. d'Amato, and R. A. Jensen. 1986. The two-isozyme system of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in Nicotiana silvestris and other higher plants. Plant Physiol. 82:203-210.
21. Genetics Computer Group, Inc. 1995. Wisconsin sequence analysis package, version 8.0. Genetics Computer Group, Inc. Madison, Wis.
22. Ger, Y., S. Chen, H. Chiang, and D. Shiuan. 1994. A single Ser-180 mutation desensitizes feedback inhibition of the phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthetase in Escherichia coli. J. Biochem. 116:986-990.
23. Ghalambor, M. A., E. M. Levine, and E. C. Heath. 1966. The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. J. Biol. Chem. 241:3207-3215.
24. Hall, G. C., M. B. Flick, R. L. Gherna, and R. A. Jensen. 1982. Biochemical diversity for biosynthesis of aromatic amino acids among the cyanobacteria. J. Bacteriol. 149:65-78.
25. Harrison, W. H., P. D. Boyer, and A. B. Falcone. 1955. The mechanism of enzymic phosphate transfer reactions. J. Biol. Chem. 215:303-317.
26. Haslam, E., R. D. Haworth, and P. F. Knowles. 1963. The preparation and identification of 5-dehydroquinic and 5-dehydroshikimic acids. Methods Enzymol. 6:498-501.
27. Hedstrom, L., and R. Abeles. 1988. 3-Deoxy-D-manno-octulosonate-8-phosphate synthase catalyzes the C - O bond cleavage of phosphoenolpyruvate. Biochem. Biophys. Res. Commun. 157:816-820.
28. Hendry, A. T. 1983. Growth responses of Neisseria gonorrhoeae auxotypes to required amino acids and bases in liquid medium. Can. J. Microbiol. 29: 1309-1313.
29. Jensen, R. A., and E. W. Nester. 1965. The regulatory significance of intermediary metabolites: control of aromatic acid biosynthesis by feedback inhibition in Bacillus subtilis. J. Mol. Biol. 12:468-481.
30. Jensen, R. A., and E. W. Nester. 1966. Regulatory enzymes of aromatic amino acid biosynthesis in Bacillus subtilis. I. Purification and properties of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase. J. Biol. Chem 241:3365-3372.
31. Kaneko, T., S. Sato, H. Kotani, A. Tanaka, E. Asamizu, Y. Nakamura, N. Miyajima, M. Hirosawa, M. Sugiura, S. Sasamoto, T. Kimura, T. Hosouchi, A. Matsuno, A. Muruki, N. Nakazaki, K. Naruo, S. Okumura, S. Shimpo, C. Takeuchi, T. Wada, A. Watanabe, M. Yamada, M. Yasuda, and S. Tabata. 1996. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3:109-136.
32. Kolibachuk, D., D. Rouhbakhsh, and P. Baumann. 1995. Aromatic amino acid biosynthesis in Buchnera aphidicola (endosymbiont of aphids): cloning and sequencing of a DNA fragment containing aroH-thrS-infC-rpmT-rplT. Curr. Microbiol. 30:313-316.
33. Künzler, M., G. Paravicini, C. M. Egli, S. Irniger, and G. H. Braus. 1992. Cloning, primary structure and regulation of the ARO4 gene, encoding the tyrosine-inhibited 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Saccharomyces cerevisiae. Gene 113:67-74.
34. Maruyama, H., R. L. Easterday, H.-C. Chang, and M. D. Lane. 1966. The enzymatic carboxylation of phosphoenolpyruvate. J. Biol. Chem. 241:2405-2412.
35. Mayer, H., U. R. Bhat, H. Masoud, J. Radziejewska-Lebrecht, C. Widemann, and J. H. Krauss. 1989. Bacterial lipopolysaccharides. Pure Appl. Chem. 61:1271-1282.
36. Mehdi, S., J. W. Frost, and J. R. Knowles. 1987. Dehydroquinate synthase from Escherichia coli and its substrate 3-deoxy-D-arabino-heptulosonic acid 7-phosphate. Methods Enzymol. 142:306-314.
37. Muday, G. K., and K. M. Herrmann. 1990. Regulation of the Salmonella typhimurium aroF gene in Escherichia coli. J. Bacteriol. 172:2259-2266.
38. Paravicini, G., H.-U. Mosch, T. Schmidheini, and G. Braus. 1989. The general control activator protein GCN4 is essential for basal ARO3 gene expression in Saccharomyces cerevisiae. Mol. Cell. Biol. 9:144-151.
39. Pereira, S. A., and G. P. Livi. 1993. Cloning and expression of the ARO3 gene encoding DAHP synthase from Candida albicans. Gene 132:159-165.
40. Ray, J. M., C. Yanofsky, and R. Bauerle. 1988. Mutational analysis of the catalytic and feedback sites of the tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase of Escherichia coli. J. Bacteriol. 170: 5500-5506.
41. Ray, P. H. 1980. Purification and characterization of 3-deoxy-D-manno-octulosonate 8-phosphate from Escherichia coli. J. Bacteriol. 141:635-644.
42. Rose, I. A., E. L. O'Connel, P. Noce, M. F. Utter, H. G. Wood, J. M. Willard, T. G. Cooper, and M. Benziman. 1969. Stereochemistry of the enzymatic carboxylation of phosphoenolpyruvate. J. Biol. Chem. 244:6120-6133.
43. Shultz, J., M. A. Hermodson, C. Garner, and K. M. Herrman. 1984. The nucleotide sequence of the aroF gene of Escherichia coli and the amino acid sequence of the encoded protein, the tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. J. Biol. Chem. 259:9655-9661.
44. Smith, L. C., J. M. Ravel, S. R. Lax, and W. Shive. 1962. The control of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthesis by phenylalanine and tyrosine. J. Biol. Chem. 237:3566-3570.
45. Srinivasan, P. R., and D. B. Sprinson. 1959. 2-Keto-3-deoxy-D-arabo-heptonic acid 7-phosphate synthetase. J. Biol. Chem. 234:716-722.
46. Stephens, C. M., and R. H. Bauerle. 1991. Analysis of the metal requirement of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli. J. Biol. Chem. 266:20810-20817.
47. Stephens, C. M., and R. Bauerle. 1992. Essential cysteines in 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Escherichia coli. J. Biol. Chem. 267:5762-5767.
48. Subramaniam P., R. Bhatnagar, A. Hooper, and R. A. Jensen. 1994. The dyamic progression of evolved character states for aromatic amino acid biosynthesis in gram-negative bacteria. Microbiology 140:3431-3440.
49. Walker, G. E., B. Dunbar, L. S. Hunter, H. G. Nimmo, and J. R. Coggins. 1996. Evidence for a novel class of microbial 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa. Microbiology 142:1973-1982.
50. Weaver, L. M., and K. M. Herrmann. 1990. Cloning of an aroF allele encoding a tyrosine-insensitive 3-deoxy-B-arabino-heptulosonate 7-phosphate synthase. J. Bacteriol. 172:6581-6584.
51. Woisetschläger, M., and G. Högenauer. 1987. The kdsA gene coding for 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase is part of an operon in Escherichia coli. Mol. Gen. Genet. 207:369-373.
52. Xia, T., G. Zhao, and R. A. Jensen. 1992. Loss of allosteric control but retention of the bifunctional catalytic competence of a fusion protein formed by excision of 260 base pairs from the 3′ terminus of PheA from Erwinia herbicola. Appl. Environ. Microbiol. 58:2792-2798.
53. Xia, T., G. Zhao, and R. A. Jensen. 1993. The pheA/tyrA/aroF region from Erwinia herbicola: an emerging comparative basis for analysis of gene organization and regulation in enteric bacteria. J. Mol. Evol. 36:107-120.