Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme a transferase involved in reduction of L-Leucine to isocaproate by Clostridium difficile
Article Abstract:
The strictly anaerobic pathogenic bacterium Clostridium difficile occurs in the human gut and is able to thrive from fermentation of leucine thus the amino acid is both oxidized to isovalerate plus [CO.sub.2] and reduced to isocaproate. In the reductive branch of this pathway, the dehydration of (R)-2-hydroxylsocaproyl-coenzyme A (CoA) to (E)-2-isocaprenoyl-CoA is probably catalyzed via radical intermediates.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2006
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Novel intermediates of acenaphthylene degradation by Rhizobium sp. strain CU-A1: Evidence for naphthalene-1,8-dicarboxylic acid metabolism
Article Abstract:
The acenaphythylene-degrading bacterium Rhizobium sp. strain CU-A1, which was isolated from petroleum-contaminated soil in Thailand, was able to degrade 600-mg/liter acenaphthylene completely within three days. The findings suggested that this strain cleaved the fused five-membered ring of acenaphthylene to form naphthalene-1,8-dicarboxylic acid via acenaphthenequinone.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2006
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