Protocatechuate 4,5-dioxygenase from Comamonas testosteroni T-2: biochemical and molecular properties of a new subgroup within class III of extradiol dioxygenases

@article{Mampel2004Protocatechuate4F,
  title={Protocatechuate 4,5-dioxygenase from Comamonas testosteroni T-2: biochemical and molecular properties of a new subgroup within class III of extradiol dioxygenases},
  author={J{\"o}rg Mampel and Miguel A. Providenti and Alasdair M. Cook},
  journal={Archives of Microbiology},
  year={2004},
  volume={183},
  pages={130-139}
}
Comamonas testosteroni T-2 degraded at least eight aromatic compounds via protocatechuate (PCA), whose extradiol ring cleavage to 2-hydroxy-4-carboxymuconate semialdehyde (HCMS) was catalysed by PCA 4,5-dioxygenase (PmdAB). This inducible, heteromultimeric enzyme was purified. It contained two subunits, α (PmdA) and β (PmdB), and the molecular masses of the denatured proteins were 18 kDa and 31 kDa, respectively. PCA was converted stoichiometrically to HCMS with an apparent Km of 55 μM and at a… CONTINUE READING

References

Publications referenced by this paper.
Showing 1-10 of 56 references

Orthanilic acid and analogues as carbon sources for bacteria: growth physiology and enzymic desulphonation

T Thurnheer, T Köhler, AM Cook, T Leisinger
J Gen Microbiol • 1986
View 6 Excerpts
Highly Influenced

Transport und Regulationsphänomene beim Abbau von 4-Toluolsulfonat in Comamonas testosteroni

J Mampel
PhD Thesis, Department of Biology, • 2000
View 5 Excerpts
Highly Influenced

Evolutionary relationships among extradiol dioxygenases.

Journal of bacteriology • 1996
View 3 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…