On the dehydration of (R)-lactate in the fermentation of alanine to propionate by Clostridium propionicum |
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Authors: | G Schweiger W Buckel |
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Institution: | 1. Department of Physics, Faculty of Science, University of Tokyo, Tokyo 113 Japan;2. Department of Chemistry, College of Science, Rikkyo (St. Paul''s) University, Nishi-Ikebukuro, Toshima-ku, Tokyo 171 Japan;3. Department of Chemistry, School of Medicine, Juntendo University, Narashino, Chiba 275 Japan;4. Mitsubishi-Kasei Institute of Life Science, Machida, Tokyo 194, Japan |
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Abstract: | All the enzymes of the pathway of (S)-alanine fermentation to acetate and propionate were detected in cell-free extracts of Clostridium propionicum . Among these (S)-glutamate dehydrogenase (NAD), (R)-lactate dehydrogenase (NAD) and propionate CoA-transferase were purified to apparent homogeneity. Their structures were presumably alpha 6, alpha 2 and alpha 4, respectively. The latter enzyme was specific for short-chain monocarboxylic acids with a pronounced preference for (R)-lactate over the (S)-enantiomer. The key step of the pathway, the dehydration of (R)-lactate required acetyl phosphate and CoASH under anaerobic conditions. It was inhibited by hydroxylamine, arsenate, azide (1 mM each) or by 0.1 mM 2,4-dinitrophenol. Thus it closely resembled the dehydration of (R)-2-hydroxyglutarate in Acidaminococcus fermentans , although an activation was not necessary. |
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Keywords: | NMR Ferredoxin 3Fe core 4Fe core Iron-sulfur |
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