1887

Abstract

Chorismate pyruvate-lyase from converts chorismate to 4-hydroxybenzoate. The enzyme was enriched 3000-fold by overexpression and chromatographic purification. It has an apparent value for chorismate of 6.1 μM and an isoelectric point of pH 6.45. The enzyme activity did not require metal cofactors. Promoter sequences in the 5′ flanking sequences of the operon were localized by transcription and translation of active chorismate pyruvate-lyase from different PCR fragments. Sequencing of the gene of the mutant strain AN244 revealed a G→A transition resulting in a change from glutamic acid to lysine. A feeding experiment with [1,7-C]shikimate confirmed the chorismate pyruvate-lyase as the sole enzymic source of 4-hydroxybenzoate .

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-140-4-897
1994-04-01
2021-08-02
Loading full text...

Full text loading...

/deliver/fulltext/micro/140/4/mic-140-4-897.html?itemId=/content/journal/micro/10.1099/00221287-140-4-897&mimeType=html&fmt=ahah

References

  1. Cho H., Heide L., Floss H.G. Synthesis of d-(-)-[l, 7-13C2]shikimic acid. J Labelled Compd & Radiopharm 1992; 31:589–594
    [Google Scholar]
  2. Chou P.Y., Fasman G.D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol 1978; 47:45–148
    [Google Scholar]
  3. Cornish-Bowden A. An automatic method for deriving steady-state rate equations. Biochem J 1977; 165:55–59
    [Google Scholar]
  4. Cornish-Bowden A., Eisenthal R. Statistical considerations in the estimation of enzyme kinetic parameters by direct linear plot and other methods. Biochem J 1974; 139:721–730
    [Google Scholar]
  5. Cox G.B., Gibson F. The role of shikimic acid in the biosynthesis of vitamin K2. Biochem J 1966; 100:1–6
    [Google Scholar]
  6. Eisenthal R., Cornish-Bowden A. The direct linear plot. Biochem J 1974; 139:715–720
    [Google Scholar]
  7. Gamier J., Osguthorpe D.J., Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol 1978; 120:97–120
    [Google Scholar]
  8. Gibson M.I., Gibson F. Preliminary studies on the isolation and metabolism of an intermediate in aromatic biosynthesis: chorismic acid. Biochem J 1964; 90:248–256
    [Google Scholar]
  9. Gottesman S., Halpern E., Trisler P. Role of sulA and sulB in filamentation by Ion mutants Escherichia coli K-12. J Bacteriol 1981; 148:265–273
    [Google Scholar]
  10. Harzer K. Analytische isoelektrische Fraktionierung der N-Acetyl-β-D-hexosaminidasen. Z Anal Chem 1970; 252:170–174
    [Google Scholar]
  11. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–685
    [Google Scholar]
  12. Lawrence J., Cox G.B., Gibson F. Biosynthesis of ubiquinone in Escherichia coli K-12: biochemical and genetic characterization of a mutant unable to convert chorismate into 4-hydroxybenzoate. J Bacteriol 1974; 118:41–45
    [Google Scholar]
  13. Lesley S.A., Brow M.A., Burgess R.R. Use of in vitro protein synthesis from polymerase chain reaction-generated templates to study interaction of Escherichia coli transcription factors with core RNA polymerase for epitope mapping of monoclonal antibodies. J Biol Chem 1991; 266:2632–2638
    [Google Scholar]
  14. Lisser S., Margalit H. Compilation of E. coli mRNA promoter sequences. Nucleic Acids Res 1993; 21:1507–1516
    [Google Scholar]
  15. Nichols B.P., Green J.M. Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase. J Bacteriol 1992; 174:5309–5316
    [Google Scholar]
  16. O'Neill M.C. Escherichia coli promoters. 1. Consensus as it relates to spacing 1989; class:specificity, repeat substructure, and threedimensional organization. J Biol Chem 264, 5522–5530
    [Google Scholar]
  17. Ozenberger B.A., Brickman T.J., McIntosh M.A. Nucleotide sequence of Escherichia coli isochorismate synthetase gene entC and evolutionary relationship of isochorismate synthetase and other chorismate-utilizing enzymes. J Bacteriol 1989; 171:775–783
    [Google Scholar]
  18. Parson W.W., Rudney H. The biosynthesis of ubiquinone and rhodoquinone from z-hydroxybenzoate and p-hydroxybenzaldehyde in Rhodospirillum rubrum. I Biol Chem 1965; 240:1855–1863
    [Google Scholar]
  19. Pennock J.F., Threlfall D.R. Biosynthesis of ubquinone and related compounds. In Biosynthesis of Isoprenoid Compounds 1983 Edited by Porter J., Spurgeon S.L. New York: Wiley; 2 pp 191–203
    [Google Scholar]
  20. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: a Laboratory Manual 1989 Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.;
    [Google Scholar]
  21. Short J.M., Fernandez J.M., Sorge J.A., Huse W. 1ZAP: a bacteriophage expression vector with in vivo excision properties. Nucleic Acids Res 1988; 16:7583–7600
    [Google Scholar]
  22. Siebert M., Bechthold A., Melzer M., May U., Berger U., Schrbder G., Schrbder J., Severin K., Heide L. Ubiquinone biosynthesis: cloning of the genes coding for chorismate pyruvate-lyase and 4-hydroxybenzoate octaprenyl transferase from Escherichia coli. FEBS Lett 1992; 307:347–350
    [Google Scholar]
  23. Stroobant P., Young I.G., Gibson F. Mutants of Escherichia coli K-12 blocked in the final reaction of ubiquinone biosynthesis: characterization and genetic analysis. J Bacteriol 1972; 109:134–139
    [Google Scholar]
  24. Wallace B.J., Young I.G. Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. studies with a ubiA- menA- double quinone mutant. Biochim Biophys Acta 1977; 461:84–100
    [Google Scholar]
  25. Walsh C.T., Liu J., Rusnak F., Sakaitani M. Molecular studies on enzymes in chorismate metabolism and the enterobactin biosynthetic pathway. Chem Rev 1990; 90:1105–1129
    [Google Scholar]
  26. Young I.G., Batterham P.J., Gibson F. The isolation, identification, and properties of isochorismic acid. An intermediate in the biosynthesis of 2,3-dihydroxybenzoic acid. Biochim Biophys Acta 1969; 177:389–400
    [Google Scholar]
  27. Young I.G., Langman L., Luke R.K., Gibson F. Biosynthesis of the iron-transport compound enterochelin: mutants of Escherichia coli unable to synthesize 2,3-dihydroxybenzoate. J Bacteriol 1971; 106:51–57
    [Google Scholar]
  28. Young I.G., Leppik R.A., Hamilton J.A., Gibson F. Biochemical and genetic studies on ubiquinone biosynthesis in Escherichia coli K-12: 4-hydroxybenzoate octaprenyltransferase. J Bacteriol 1972; 110:18–25
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-140-4-897
Loading
/content/journal/micro/10.1099/00221287-140-4-897
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error