Enzymes involved in crotonate metabolism in Syntrophomonas wolfei
- Univ. of Oklahoma, Norman, OK (United States). Dept. of Botany and Microbiology
Cell-free extracts of Syntrophomonas wolfei subsp. wolfei grown with crotonate in pure culture or in coculture with Methanospirillum hungatei contained crotonyl-coenzyme A (CoA):acetate CoA-transferase activity. This activity was not detected in cell-free extracts from the butyrate-grown coculture which suggests that the long lag times observed before S. wolfei grew with crotonate were initially due to the inability to activate crotonate. Cell-free extracts of S. wolfei grown in pure culture contained high specific activities of hydrogenase and very low levels of formate dehydrogenase. The low levels suggest a biosynthetic rather than a catabolic role for the latter enzyme when S. wolfei is grown in pure culture. CO dehydrogenase activity was not detected. S. wolfei can form butyrate using a CoA transferase activity, but not by a phosphotransbutyrylase or enoate reductase activity. A c-type cytochrome was detected in S. wolfei grown in pure culture or in coculture indicating the presence of an electron transport system. This is a characteristic which separates S. wolfei from other known crotonate-using bacteria.
- Sponsoring Organization:
- USDOE, Washington, DC (United States)
- DOE Contract Number:
- FG05-89ER14003
- OSTI ID:
- 514561
- Journal Information:
- Archives of Microbiology, Vol. 158; Other Information: PBD: 1992
- Country of Publication:
- United States
- Language:
- English
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