Sulphoacetaldehyde acetyltransferase yields acetyl phosphate : purification from Alcaligenes defragrans and gene clusters in taurine degradation

Ruff, Jürgen; Denger, Karin; Cook, Alasdair M.

Sulphoacetaldehyde acetyltransferase yields acetyl phosphate : purification from Alcaligenes defragrans and gene clusters in taurine degradation

Dateien

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Datum

2003

Autor:innen

Ruff, Jürgen

Denger, Karin

Cook, Alasdair M.

URI (zitierfähiger Link)

http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-67123

Link zur Lizenz

Attribution-NonCommercial-NoDerivs 2.0 Generic

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Biochemical Journal. 2003, 369(2), pp. 275-285. ISSN 0264-6021. eISSN 1470-8728

Zusammenfassung

The facultatively anaerobic bacterium Alcaligenes defragrans NKNTAU was found to oxidize taurine (2-aminoethanesulphonate) with nitrate as the terminal electron acceptor. Taurine was transaminated to 2-sulphoacetaldehyde. This was not converted into sulphite and acetate by a "sulphoacetaldehyde sulpho-lyase" (EC 4.4.1.12), but into sulphite and acetyl phosphate, which was identified by three methods. The enzyme, which required the addition of phosphate, thiamin diphosphate and Mg(2+) ions for activity, was renamed sulphoacetaldehyde acetyltransferase (Xsc; EC 2.3.1.-). Inducible Xsc was expressed at high levels, and a three-step 11-fold purification yielded an essentially homogeneous soluble protein, which was a homotetramer in its native form; the molecular mass of the subunit was found to be between about 63 kDa (SDS/PAGE) and 65.3 kDa (matrix-assisted laser-desorption ionization-time-of-flight MS). The N-terminal and two internal amino acid sequences were determined, and PCR primers were generated. The xsc gene was amplified and sequenced; the derived molecular mass of the processed protein was 65.0 kDa. The downstream gene presumably encoded the inducible phosphate acetyltransferase (Pta) found in crude extracts. The desulphonative enzymes ("EC 4.4.1.12") from Achromobacter xylosoxidans NCIMB 10751 and Desulfonispora thiosulfatigenes GKNTAU were shown to be Xscs. We detected at least three subclasses of xsc in Proteobacteria and in Gram-positive bacteria, and they comprised a distinct group within the acetohydroxyacid synthase supergene family. Genome sequencing data revealed xsc genes in Burkholderia fungorum (80% sequence identity) and Sinorhizobium meliloti (61%) with closely linked pta genes. Different patterns of regulation for the transport and dissimilation of taurine were hypothesized for S. meliloti and B. fungorum.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

desulphonation, phosphate acetyltransferase, sequence comparison, sulphoacetaldehyde sulpho-lyase, thiamin diphosphate

Zitieren

ISO 690

RUFF, Jürgen, Karin DENGER, Alasdair M. COOK, 2003. Sulphoacetaldehyde acetyltransferase yields acetyl phosphate : purification from Alcaligenes defragrans and gene clusters in taurine degradation. In: Biochemical Journal. 2003, 369(2), pp. 275-285. ISSN 0264-6021. eISSN 1470-8728

BibTex

@article{Ruff2003Sulph-8667,
  year={2003},
  title={Sulphoacetaldehyde acetyltransferase yields acetyl phosphate : purification from Alcaligenes defragrans and gene clusters in taurine degradation},
  number={2},
  volume={369},
  issn={0264-6021},
  journal={Biochemical Journal},
  pages={275--285},
  author={Ruff, Jürgen and Denger, Karin and Cook, Alasdair M.}
}

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    <dcterms:abstract xml:lang="eng">The facultatively anaerobic bacterium Alcaligenes defragrans NKNTAU was found to oxidize taurine (2-aminoethanesulphonate) with nitrate as the terminal electron acceptor. Taurine was transaminated to 2-sulphoacetaldehyde. This was not converted into sulphite and acetate by a "sulphoacetaldehyde sulpho-lyase" (EC 4.4.1.12), but into sulphite and acetyl phosphate, which was identified by three methods. The enzyme, which required the addition of phosphate, thiamin diphosphate and Mg(2+) ions for activity, was renamed sulphoacetaldehyde acetyltransferase (Xsc; EC 2.3.1.-). Inducible Xsc was expressed at high levels, and a three-step 11-fold purification yielded an essentially homogeneous soluble protein, which was a homotetramer in its native form; the molecular mass of the subunit was found to be between about 63 kDa (SDS/PAGE) and 65.3 kDa (matrix-assisted laser-desorption ionization-time-of-flight MS). The N-terminal and two internal amino acid sequences were determined, and PCR primers were generated. The xsc gene was amplified and sequenced; the derived molecular mass of the processed protein was 65.0 kDa. The downstream gene presumably encoded the inducible phosphate acetyltransferase (Pta) found in crude extracts. The desulphonative enzymes ("EC 4.4.1.12") from Achromobacter xylosoxidans NCIMB 10751 and Desulfonispora thiosulfatigenes GKNTAU were shown to be Xscs. We detected at least three subclasses of xsc in Proteobacteria and in Gram-positive bacteria, and they comprised a distinct group within the acetohydroxyacid synthase supergene family. Genome sequencing data revealed xsc genes in Burkholderia fungorum (80% sequence identity) and Sinorhizobium meliloti (61%) with closely linked pta genes. Different patterns of regulation for the transport and dissimilation of taurine were hypothesized for S. meliloti and B. fungorum.</dcterms:abstract>
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