Publikation: Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum
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2000
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Archives of Microbiology. 2000, 173(4), pp. 288-295. ISSN 0302-8933. eISSN 1432-072X. Available under: doi: 10.1007/s002030000148
Zusammenfassung
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
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Anaerobic degradation, Aromatic compounds, 3-Hydroxybenzoate, Benzoyl-CoA pathway, Reductive dehydroxylation, Fermenting bacteria
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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/s002030000148BibTex
@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}
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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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