Skip to main content
SpringerLink
Log in

3,4-Dihydroxyphenylacetate 2,3-dioxygenase

  • Chapter
Springer Handbook of Enzymes

Part of the book series: Springer Handbook of Enzymes ((HDBKENZYMES,volume 25))

  • 75 Accesses

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 259.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 329.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 329.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Nozaki, M.: Nonheme iron dioxygenase. Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York, 135–165 (1974)

    Google Scholar 

  2. Jenkins, J.R.; Cooper, R.A.: Molecular cloning, expression, and analysis of the genes of the homoprotocatechuate catabolic pathway of Escherichia coli C. J. Bacteriol., 170, 5317–5324 (1988)

    PubMed  CAS  Google Scholar 

  3. Roper, D.I.; Cooper, R.A.: Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C. FEBS Lett., 275, 53–57 (1990)

    Article  PubMed  CAS  Google Scholar 

  4. Blakley, E.R.: The catabolism of l-tyrosine by an Arthrobacter sp.. Can. J. Microbiol., 23, 1128–1139 (1977)

    Article  PubMed  CAS  Google Scholar 

  5. Kutty, R.K.; Devi, N.A.; Veeraswamy, M.; Ramesh, S.; Rao, P.V.S.: Degradation of (+/−)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde. Biochem. J., 167, 163–170 (1977)

    PubMed  CAS  Google Scholar 

  6. Barbour, M.G.; Bayly, R.C.: Regulation of the 4-hydroxyphenylacetic acid meta-cleavage pathway in an Acinetobacter sp. Biochem. Biophys. Res. Commun., 79, 663–670 (1977)

    Article  PubMed  CAS  Google Scholar 

  7. Mayer, R.; Widom, J.; Que, L.: Involvement of superoxide in the reactions of the catechol dioxygenases. Biochem. Biophys. Res. Commun., 92, 285–291 (1980)

    Article  PubMed  CAS  Google Scholar 

  8. Cooper, R.A.; Skinner, M.A.: Catabolism of 3-and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coil. J. Bacteriol., 143, 302–306 (1980)

    PubMed  CAS  Google Scholar 

  9. Klages, U.; Markus, A.; Lingens, E: Degradation of 4-chlorophenylacetic acid by a Pseudomonas species. J. Bacteriol., 146, 64–68 (1981)

    PubMed  CAS  Google Scholar 

  10. Barbour, M.G.; Bayly, R.C.: Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida. J. Bacteriol., 147, 844–850 (1981)

    PubMed  CAS  Google Scholar 

  11. Adachi, K.; Takeda, Y.; Senoh, S.; Kita, H.: Metabolism of p-hydroxyphenyl-acetic acid in Pseudomonas ovalis. Biochim. Biophys. Acta, 93, 483–493 (1964)

    PubMed  CAS  Google Scholar 

  12. Lee, Y.L.; Dagley, S.: Comparison of two dioxygenases from Pseudomonas putida. J. Bacteriol., 131, 1016–1017 (1977)

    CAS  Google Scholar 

  13. Barbour, M.G.; Bayly, R.C.: Regulation of the meta-cleavage of 4-hydroxyphenylacetic acid by Pseudomonas putida. Biochem. Biophys. Res. Commun., 76, 565–571 (1977)

    Article  CAS  Google Scholar 

  14. Que, L.; Widom, J.; Crawford, R.L.: 3,4-Dihydroxyphenylacetate 2,3-dioxygenase. A manganese(II) dioxygenase from Bacillus brevis. J. Biol. Chem., 256, 10941–10944 (1981)

    PubMed  CAS  Google Scholar 

  15. Lee, C.W.; Lucas, S.; Desmazeaud, M.J.: Phenylalanine and tyrosine catabolism in some cheese coryneform bacteria. FEMS Microbiol. Lett., 26, 201–205 (1985)

    Article  CAS  Google Scholar 

  16. Trias, J.; Vinas, M.; Guinea, J.; Loren, J.G.: Isolation from urine of two Serratia marcescens strains excreting a diffusible yellow pigment. J. Gen. Microbiol., 133, 773–777 (1987)

    PubMed  CAS  Google Scholar 

  17. Cuskey, S.M.; Olsen, R.H.: Catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO1 via meta cleavage of homoprotocatechuic acid. J. Bacteriol., 170, 393–399 (1988)

    PubMed  CAS  Google Scholar 

  18. Jamaluddin, M.P.: Purification and properties of homoprotocatechuate 2,3-dioxygenase from Bacillus stearothermophilus. J. Bacteriol., 129, 690–697 (1977)

    PubMed  CAS  Google Scholar 

  19. Sparnins, V.L.; Chapman, P.J.: Catabolism of l-tyrosine by the homoprotocatechuate pathway in gram-positive bacteria. J. Bacteriol., 127, 362–366 (1976)

    PubMed  CAS  Google Scholar 

  20. Sparnins, V.L.; Chapman, P.J.; Dagley, S.: Bacterial degradation of 4-hydroxyphenylacetic acid and homoprotocatechuic acid. J. Bacteriol., 120, 159–167 (1974)

    PubMed  CAS  Google Scholar 

  21. Ono-Kamimoto, M.: Studies on 3,4-dihydroxyphenylacetate 2,3-dioxygenase. I. Role of iron, substrate binding, and some other properties. J. Biochem., 74, 1049–1059 (1973)

    PubMed  CAS  Google Scholar 

  22. Ono-Kamimoto, M.; Senoh, S.: Studies on 3,4-dihydroxyphenylacetate-2,3-dioxygenase. II. Role of sulfhydryl groups and subunit structure. J. Biochem., 75, 321–331 (1974)

    PubMed  CAS  Google Scholar 

  23. Miller, M.A.; Lipscomb, J.D.: Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity. J. Biol. Chem., 271, 5524–5535 (1996)

    Article  PubMed  CAS  Google Scholar 

  24. Boldt, Y.R.; Whiting, A.K.; Wagner, M.L.; Sadowsky, M.J.; Que, L., Jr.; Wackett, L.P.: Manganese(II) active site mutants of 3,4-dihydroxyphenylacetate 2,3-dioxygenase from Arthrobacter globiformis strain CM-2. Biochemistry, 36, 2147–2153 (1997)

    Article  PubMed  CAS  Google Scholar 

  25. Wang, Y.Z.; Lipscomb, J.D.: Cloning, overexpression, and mutagenesis of the gene for homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. Protein Expr. Purif., 10, 1–9 (1997)

    Article  PubMed  CAS  Google Scholar 

  26. Gibello, A.; Ferrer, E.; Martin, M.; Garrido-Pertierra, A.: 3,4-Dihydroxyphenylacetate 2,3-dioxygenase from Klebsiella pneumoniae, a Mg2+-containing dioxygenase involved in aromatic catabolism. Biochem. J., 301, 145–150 (1994)

    PubMed  CAS  Google Scholar 

Download references

Editor information

Editors and Affiliations

  1. Institute for Biochemistry, University to Cologne, Zülpicher Strasse 47, 50674, Cologne, Germany

    Dietmar Schomburg  & Ida Schomburg  & 

Rights and permissions

Reprints and permissions

Copyright information

© 2006 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

(2006). 3,4-Dihydroxyphenylacetate 2,3-dioxygenase. In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 25. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37704-2_61

Download citation

Publish with us

Policies and ethics

Search

Navigation