Enzymes and genes of taurine and isethionate dissimilation in Paracoccus denitrificans.
Growth of the alpha-proteobacterium Paracoccus denitrificans NKNIS with taurine or isethionate as sole source of carbon involves sulfoacetaldehyde acetyltransferase (Xsc), which is presumably encoded by an xsc gene in subgroup 3, none of whose gene products has been characterized. The genome of the alpha-proteobacterium Rhodobacter sphaeroides 2.4.1 was interpreted to contain a nine-gene cluster encoding the inducible dissimilation of taurine, and this deduced pathway included a regulator, a tripartite ATP-independent transporter, taurine dehydrogenase (TDH; presumably TauXY) as well as Xsc (subgroup 3), a hypothetical protein and phosphate acetyltransferase (Pta). A similar cluster was found in P. denitrificans NKNIS, in contrast to an analogous cluster encoding an ATP-binding cassette transporter in Paracoccus pantotrophus. Inducible TDH, Xsc and Pta were found in extracts of taurine-grown cells of strain NKNIS. TDH oxidized taurine to sulfoacetaldehyde and ammonium ion with cytochrome c as electron acceptor. Whereas Xsc and Pta were soluble enzymes, TDH was located in the particulate fraction, where inducible proteins with the expected masses of TauXY (14 and 50 kDa, respectively) were detected by SDS-PAGE. Xsc and Pta were separated by anion-exchange chromatography. Xsc was effectively pure; the molecular mass of the subunit (64 kDa) and the N-terminal amino acid sequence confirmed the identification of the xsc gene. Inducible isethionate dehydrogenase (IDH), Xsc and Pta were assayed in extracts of isethionate-grown cells of strain NKNIS. IDH was located in the particulate fraction, oxidized isethionate to sulfoacetaldehyde with cytochrome c as electron acceptor and correlated with the expression of a 62 kDa protein. Strain NKNIS excreted sulfite and sulfate during growth with a sulfonate and no sulfite dehydrogenase was detected. There is considerable biochemical, genetic and regulatory complexity in the degradation of these simple molecules.
Brüggemann
Chantal
C
Department of Biology, The University, D-78457 Konstanz, Germany.
Denger
Karin
K
Department of Biology, The University, D-78457 Konstanz, Germany.
Cook
Alasdair M
AM
Department of Biology, The University, D-78457 Konstanz, Germany.
Ruff
Jürgen
J
Department of Biology, The University, D-78457 Konstanz, Germany.
D000079:Acetaldehyde / Q000031:analogs & derivatives* / Q000378:metabolism; D000123:Acetyltransferases / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D007513:Isethionic Acid / Q000378:metabolism*; D008969:Molecular Sequence Data; D005810:Multigene Family; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000235:genetics / Q000378:metabolism; D010231:Paracoccus denitrificans / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D010709:Phosphate Acetyltransferase / Q000235:genetics / Q000378:metabolism; D041902:Rhodobacteraceae / Q000201:enzymology / Q000235:genetics; D017422:Sequence Analysis, DNA; D013654:Taurine / Q000378:metabolism*
D001426:Bacterial Proteins; D013654:Taurine; C015517:sulfoacetaldehyde; D007513:Isethionic Acid; D010088:Oxidoreductases; C053682:taurine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D000123:Acetyltransferases; D010709:Phosphate Acetyltransferase; D000079:Acetaldehyde