Publikation: Roseovarius sp. strain 217 : aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase
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2007
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FEMS Microbiology Letters. 2007, 271(2), pp. 202-206. ISSN 0378-1097. eISSN 1574-6968. Available under: doi: 10.1111/j.1574-6968.2007.00719.x
Zusammenfassung
The genome sequence of Roseovarius sp. strain 217 indicated that many pathway enzymes found in other organisms for the degradation of taurine are represented, but that a novel, apparently energy-dependent pathway is involved in the conversion of acetyl phosphate to acetyl CoA. Thus, an ABC transporter for taurine could be postulated, while inducible taurine: pyruvate aminotransferase, alanine dehydrogenase, sulfoacetaldehyde acetyltransferase and sulfite dehydrogenase could be assayed. Whereas phosphate acetyltransferase has been found in other organisms, none was indicated in the genome sequence and no activity was found in cell-free extracts. Instead, acetate kinase was active as was acetate-CoA ligase.
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Fachgebiet (DDC)
570 Biowissenschaften, Biologie
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acetate:CoA ligase (AMP-forming), acetate kinase, Burkholderia xenovorans LB400, genome sequences, Roseovarius sp. strain 217
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BALDOCK, Marijke I., Karin DENGER, Theo H. M. SMITS, Alasdair M. COOK, 2007. Roseovarius sp. strain 217 : aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase. In: FEMS Microbiology Letters. 2007, 271(2), pp. 202-206. ISSN 0378-1097. eISSN 1574-6968. Available under: doi: 10.1111/j.1574-6968.2007.00719.xBibTex
@article{Baldock2007Roseo-7572,
year={2007},
doi={10.1111/j.1574-6968.2007.00719.x},
title={Roseovarius sp. strain 217 : aerobic taurine dissimilation via acetate kinase and acetate-CoA ligase},
number={2},
volume={271},
issn={0378-1097},
journal={FEMS Microbiology Letters},
pages={202--206},
author={Baldock, Marijke I. and Denger, Karin and Smits, Theo H. M. and Cook, Alasdair M.}
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<dcterms:abstract xml:lang="eng">The genome sequence of Roseovarius sp. strain 217 indicated that many pathway enzymes found in other organisms for the degradation of taurine are represented, but that a novel, apparently energy-dependent pathway is involved in the conversion of acetyl phosphate to acetyl CoA. Thus, an ABC transporter for taurine could be postulated, while inducible taurine: pyruvate aminotransferase, alanine dehydrogenase, sulfoacetaldehyde acetyltransferase and sulfite dehydrogenase could be assayed. Whereas phosphate acetyltransferase has been found in other organisms, none was indicated in the genome sequence and no activity was found in cell-free extracts. Instead, acetate kinase was active as was acetate-CoA ligase.</dcterms:abstract>
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