Archives of Microbiology

, Volume 158, Issue 5, pp 344–349

Enzymes involved in crotonate metabolism in Syntrophomonas wolfei

Authors

  • Michael J. McInerney
    • Department of Botany and MicrobiologyUniversity of Oklahoma
  • Neil Q. Wofford
    • Department of Botany and MicrobiologyUniversity of Oklahoma
Original Papers

DOI: 10.1007/BF00245363

Cite this article as:
McInerney, M.J. & Wofford, N.Q. Arch. Microbiol. (1992) 158: 344. doi:10.1007/BF00245363

Abstract

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 biosynthethic 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.

Key words

Methanogenesis Syntrophy Anaerobic fatty acid degradation Crotonate β-Oxidation CoA transferase

Copyright information

© Springer-Verlag 1992