L-Cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T)

Denger, Karin; Smits, Theo H. M.; Cook, Alasdair M.

L-Cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T)

Dateien

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Datum

2006

Autor:innen

Denger, Karin

Smits, Theo H. M.

Cook, Alasdair M.

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Biochemical Journal. 2006, 394(3), pp. 657-664. ISSN 0264-6021. eISSN 1470-8728. Available under: doi: 10.1042/BJ20051311

Zusammenfassung

Quantitative utilization of L-cysteate (2-amino-3-sulphopropionate) as the sole source of carbon and energy for growth of the aerobic, marine bacterium Silicibacter pomeroyi DSS-3(T) was observed. The sulphonate moiety was recovered in the medium largely as sulphite, and the appropriate amount of the ammonium ion was also observed. Genes [suyAB (3-sulpholactate sulpho-lyase)] encoding the known desulphonation reaction in cysteate degradation were absent from the genome, but a homologue of a putative sulphate exporter gene (suyZ) was found, and its neighbour, annotated as a D-cysteine desulphhydrase, was postulated to encode pyridoxal 5'-phosphate-coupled L-cysteate sulpho-lyase (CuyA), a novel enzyme. Inducible CuyA was detected in cysteate-grown cells. The enzyme released equimolar pyruvate, sulphite and the ammonium ion from L-cysteate and was purified to homogeneity by anion-exchange, hydrophobic-interaction and gel-filtration chromatography. The N-terminal amino acid sequence of this 39-kDa subunit confirmed the identification of the cuyA gene. The native enzyme was soluble and homomultimeric. The K(m)-value for L-cysteate was high (11.7 mM) and the enzyme also catalysed the D-cysteine desulphhydrase reaction. The gene cuyZ, encoding the putative sulphite exporter, was co-transcribed with cuyA. Sulphite was exported despite the presence of a ferricyanide-coupled sulphite dehydrogenase. CuyA was found in many bacteria that utilize cysteate.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

cysteate dissimilation, desulphonation, pyridoxal 5'-phosphate, sequence comparisons, sulphite exporter

Zitieren

ISO 690

DENGER, Karin, Theo H. M. SMITS, Alasdair M. COOK, 2006. L-Cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T). In: Biochemical Journal. 2006, 394(3), pp. 657-664. ISSN 0264-6021. eISSN 1470-8728. Available under: doi: 10.1042/BJ20051311

BibTex

@article{Denger2006LCyst-8480,
  year={2006},
  doi={10.1042/BJ20051311},
  title={L-Cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T)},
  number={3},
  volume={394},
  issn={0264-6021},
  journal={Biochemical Journal},
  pages={657--664},
  author={Denger, Karin and Smits, Theo H. M. and Cook, Alasdair M.}
}

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