Acta Biologica Hungarica

, Volume 58, Supplement 1, pp 37–49 | Cite as

Overlaps between the Various Biodegradation Pathways in sphingomonas Subarctica SA1

  • Mónika Magony
  • Ildikó Kákonyi
  • Anna Gara
  • P. Rapali
  • Katalin Perei
  • K. L. Kovács
  • G. RákhelyEmail author


A bacterium capable to grow on sulfanilic acid as sole carbon, nitrogen and sulfur source has been isolated. A unique feature of this strain is that it contains the full set of enzymes necessary for the biodegra-dation of sulfanilic acid. Taxonomical analysis identified our isolate as Sphingomonas subarctica SA1 sp. The biodegradation pathway of sulfanilic acid was investigated at the molecular level. Screening the substrate specificity of the strain disclosed its capacity to degrade six analogous aromatic compounds including p-aminobenzoic acid. Moreover, the strain was successfully used for removal of oil contaminations. S. subarctica SA1 seemed to use distinct enzyme cascades for decomposition of these molecules, since alternative enzymes were induced in cells grown on various substrates. However, the protein patterns appearing upon induction by sulfanilic acid and sulfocatechol were very similar to each other indicating common pathways for the degradation of these substrates. Cells grown on sulfanilic acid could convert p-aminobenzoic acid to some extent and vice versa. Two types of ring cleaving dioxygenases were detected in the cells grown on various substrates: one preferred protocatechol, while the other had higher activity with sulfocatechol. This latter enzyme, named as sulfocatechol dioxygenase was partially purified and characterized.


Biodegradation dioxygenase Sphingomonas subarctica sulfanilic acid 



3,5-dihydroxybenzoic acid


4-hydroxybenzoic acid


p-aminobenzoic acid




sulfanilic acid




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© Akadémiai Kiadó, Budapest 2007

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Authors and Affiliations

  • Mónika Magony
    • 1
  • Ildikó Kákonyi
    • 1
  • Anna Gara
    • 1
  • P. Rapali
    • 1
  • Katalin Perei
    • 1
  • K. L. Kovács
    • 1
  • G. Rákhely
    • 1
    • 2
    Email author
  1. 1.Department of BiotechnologyUniversity of SzegedSzegedHungary
  2. 2.Institute of Biophysics, Biological Research CenterHungarian Academy of SciencesSzegedHungary

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