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Microbiology 145 (1999), 1153-1160
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microbiology, Vol 145, 1153-1160, Copyright © 1999 by Society for General Microbiology

ARTICLES

Anaerobic oxidations of cysteate: degradation via L-cysteate:2-oxoglutarate aminotransferase in Paracoccus pantotrophus

CARM Mikosch, K Denger, EM Schafer and AM Cook
Department of Biology, The University, D-78457 Konstanz, Germany

Anoxic, fresh-water enrichment cultures to oxidize different organosulfonates were set up with nitrate, ferric iron or sulfate as electron acceptors. Pure cultures were easily obtained with two naturally occurring sulfonates, cysteate (2-amino-3-sulfopropionate) and taurine (2-aminoethanesulfonate), under nitrate-reducing conditions. These two sulfonates were also oxidized during reduction of iron(III), though isolation of pure cultures was not successful. One nitrate-reducing cysteate-oxidizing bacterium, strain NKNCYSA, was studied in detail. It was identified as Paracoccus pantotrophus. Eighteen sulfonates were tested, and the organism degraded cysteate, taurine, isethionate (2-hydroxyethanesulfonate), sulfoacetate or 3-amino-propanesulfonate with concomitant reduction of nitrate, presumably to molecular nitrogen. The carbon skeleton of these substrates was converted to cell material and, presumably, CO2. The amino group was released as ammonia and the sulfono moiety was recovered as sulfate. Cell-free extracts of P. pantotrophus NKNCYSA contained constitutive L-cysteate:2-oxoglutarate aminotransferase (EC 2.6.1.--) and glutamate dehydrogenase (EC 1.4.1.4). Taurine:pyruvate aminotransferase, in contrast, was inducible.


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U. Rein, R. Gueta, K. Denger, J. Ruff, K. Hollemeyer, and A. M. Cook
Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA
Microbiology, March 1, 2005; 151(3): 737 - 747.
[Abstract] [Full Text] [PDF]

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C. Bruggemann, K. Denger, A. M. Cook, and J. Ruff
Enzymes and genes of taurine and isethionate dissimilation in Paracoccus denitrificans
Microbiology, April 1, 2004; 150(4): 805 - 816.
[Abstract] [Full Text] [PDF]


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