Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum
| dc.contributor.author | Müller, Jochen A. | |
| dc.contributor.author | Schink, Bernhard | |
| dc.date.accessioned | 2011-03-24T17:41:09Z | deu |
| dc.date.available | 2011-03-24T17:41:09Z | deu |
| dc.date.issued | 2000 | deu |
| dc.description.abstract | The anaerobic bacterium Sporotomaculum hydroxybenzoicum ferments 3-hydroxybenzoate to acetate, butyrate, and CO2. 3-Hydroxybenzoate was activated to 3-hydroxybenzoyl-CoA in a CoA-transferase reaction with acetyl-CoA or butyryl-CoA as CoA donors. 3-Hydroxybenzoyl-CoA was reductively dehydroxylated, forming benzoyl-CoA. This reaction was measured in cell-free extracts with cob(I)alamin as low-potential electron donor. No evidence was obtained that cob(I)alamin is the physiological electron donor; however, inhibitor studies indicated involvement of a strong nucleophile in the reaction. Benzoate was degraded by dense cell suspensions without a lag phase until an in situ DG¢ value | eng |
| dc.description.version | published | |
| dc.format.mimetype | application/pdf | deu |
| dc.identifier.citation | First publ. in: Archives of Microbiology 173 (2000), 4, pp. 288-295 | deu |
| dc.identifier.doi | 10.1007/s002030000148 | |
| dc.identifier.ppn | 263903818 | deu |
| dc.identifier.uri | http://kops.uni-konstanz.de/handle/123456789/8173 | |
| dc.language.iso | eng | deu |
| dc.legacy.dateIssued | 2007 | deu |
| dc.rights | Attribution-NonCommercial-NoDerivs 2.0 Generic | |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/2.0/ | |
| dc.subject | Anaerobic degradation | deu |
| dc.subject | Aromatic compounds | deu |
| dc.subject | 3-Hydroxybenzoate | deu |
| dc.subject | Benzoyl-CoA pathway | deu |
| dc.subject | Reductive dehydroxylation | deu |
| dc.subject | Fermenting bacteria | deu |
| dc.subject.ddc | 570 | deu |
| dc.title | Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum | eng |
| dc.type | JOURNAL_ARTICLE | deu |
| dspace.entity.type | Publication | |
| kops.citation.bibtex | @article{Muller2000Initi-8173,
year={2000},
doi={10.1007/s002030000148},
title={Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum},
number={4},
volume={173},
issn={0302-8933},
journal={Archives of Microbiology},
pages={288--295},
author={Müller, Jochen A. and Schink, Bernhard}
} | |
| kops.citation.iso690 | MÜLLER, Jochen A., Bernhard SCHINK, 2000. Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum. In: Archives of Microbiology. 2000, 173(4), pp. 288-295. ISSN 0302-8933. eISSN 1432-072X. Available under: doi: 10.1007/s002030000148 | deu |
| kops.citation.iso690 | MÜLLER, Jochen A., Bernhard SCHINK, 2000. Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum. In: Archives of Microbiology. 2000, 173(4), pp. 288-295. ISSN 0302-8933. eISSN 1432-072X. Available under: doi: 10.1007/s002030000148 | eng |
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<dcterms:abstract xml:lang="eng">The anaerobic bacterium Sporotomaculum hydroxybenzoicum ferments 3-hydroxybenzoate to acetate, butyrate, and CO2. 3-Hydroxybenzoate was activated to 3-hydroxybenzoyl-CoA in a CoA-transferase reaction with acetyl-CoA or butyryl-CoA as CoA donors. 3-Hydroxybenzoyl-CoA was reductively dehydroxylated, forming benzoyl-CoA. This reaction was measured in cell-free extracts with cob(I)alamin as low-potential electron donor. No evidence was obtained that cob(I)alamin is the physiological electron donor; however, inhibitor studies indicated involvement of a strong nucleophile in the reaction. Benzoate was degraded by dense cell suspensions without a lag phase until an in situ DG¢ value</dcterms:abstract>
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| source.periodicalTitle | Archives of Microbiology |
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