Sulfoacetate Is Degraded via a Novel Pathway Involving Sulfoacetyl-CoA and Sulfoacetaldehyde in Cupriavidus necator H16

Weinitschke, Sonja; Hollemeyer, Klaus; Kusian, Bernhard; Bowien, Botho; Smits, Theo H. M.; Cook, Alasdair M.

Sulfoacetate Is Degraded via a Novel Pathway Involving Sulfoacetyl-CoA and Sulfoacetaldehyde in Cupriavidus necator H16

Dateien

Weinitschke_Sulfoacetate_JBC_2010.pdfGröße: 603.94 KBDownloads: 222

Datum

2010

Autor:innen

Weinitschke, Sonja

Hollemeyer, Klaus

Kusian, Bernhard

Bowien, Botho

Smits, Theo H. M.

Cook, Alasdair M.

Verlag

Bethesda, Md. : Soc.

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

The Journal of Biological Chemistry. 2010, 285(46), pp. 35249-35254. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M110.127043

Zusammenfassung

Bacterial degradation of sulfoacetate, a widespread natural product, proceeds via sulfoacetaldehyde and requires a considerable initial energy input. Whereas the fate of sulfoacetaldehyde in Cupriavidus necator (Ralstonia eutropha) H16 is known, the pathway from sulfoacetate to sulfoacetaldehyde is not. The genome sequence of the organism enabled us to hypothesize that the inducible pathway, which initiates sau (sulfoacetate utilization), involved a four-gene cluster (sauRSTU; H16_A2746 to H16_A2749). The sauR gene, divergently orientated to the other three genes, probably encodes the transcriptional regulator of the presumed sauSTU operon, which is subject to inducible transcription. SauU was tentatively identified as a transporter of the major facilitator superfamily, and SauT was deduced to be a sulfoacetate-CoA ligase. SauT was a labile protein, but it could be separated and shown to generate AMP and an unknown, labile CoA-derivative from sulfoacetate, CoA, and ATP. This unknown compound, analyzed by MALDI-TOF-MS, had a relative molecular mass of 889.7, which identified it as protonated sulfoacetyl-CoA (calculated 889.6). SauS was deduced to be sulfoacetaldehyde dehydrogenase (acylating). The enzyme was purified 175-fold to homogeneity and characterized. Peptide mass fingerprinting confirmed the sauS locus (H16_A2747). SauS converted sulfoacetyl-CoA and NADPH to sulfoacetaldehyde, CoA, and NADP+, thus confirming the hypothesis.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

Anion Transport, Bacterial Metabolism, Coenzyme A, Dehydrogenase, Enzyme Purification, Gene Knockout, Cupriavidus necator, Sulfoacetaldehyde, Sulfoacetate, Sulfoacetyl-CoA

Zitieren

ISO 690

WEINITSCHKE, Sonja, Klaus HOLLEMEYER, Bernhard KUSIAN, Botho BOWIEN, Theo H. M. SMITS, Alasdair M. COOK, 2010. Sulfoacetate Is Degraded via a Novel Pathway Involving Sulfoacetyl-CoA and Sulfoacetaldehyde in Cupriavidus necator H16. Bethesda, Md. : Soc.. In: The Journal of Biological Chemistry. 2010, 285(46), pp. 35249-35254. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M110.127043

BibTex

@article{Weinitschke2010Sulfo-13544,
  year={2010},
  doi={10.1074/jbc.M110.127043},
  title={Sulfoacetate Is Degraded via a Novel Pathway Involving Sulfoacetyl-CoA and Sulfoacetaldehyde in Cupriavidus necator H16},
  number={46},
  volume={285},
  issn={0021-9258},
  journal={The Journal of Biological Chemistry},
  pages={35249--35254},
  author={Weinitschke, Sonja and Hollemeyer, Klaus and Kusian, Bernhard and Bowien, Botho and Smits, Theo H. M. and Cook, Alasdair M.}
}

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Universitätsbibliographie

Ja