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Title of Journal: FEMS Microbiol Lett

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Abbravation: FEMS Microbiology Letters

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Narnia

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DOI

10.1007/bfb0089939

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0378-1097

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Purification of an enzyme responsible for acetate

Authors: Michel Tomas A Macy Joan M
Publish Date: 1990/03/01
Volume: 68, Issue: 1-2, Pages: 189-194
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Abstract

Tomas A Michel Joan M Macy Purification of an enzyme responsible for acetate formation from acetyl coenzyme A in Selenomonas ruminantium FEMS Microbiology Letters Volume 68 Issue 12 March 1990 Pages 189–194 https//doiorg/101111/j157469681990tb04147xAn enzyme capable of catalyzing the ADPdependent conversion of acetyl coenzyme A propionyl coenzyme A and succinyl coenzyme A into the corresponding free acids has been purified from the strict rumen anaerobe Selenomonas ruminantium All three activities cochromatographed and have been purified 60fold As determined by gel filtration the molecular weight of this enzyme was 230 000 Gel electrophoresis in native gels resolved the purified protein fraction into a major and three minor protein bands The relative mobility of the major band coincided with the relative mobility of single bands that were obtained when gels were stained for activity with each of the three substrates The physiological role of this new enzyme is discussed

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References

citation author=Reeves RE citation author=Warren LG citation author=Susskind B citation author=Lo HS citation journal title=J Biol Chem citation year=1977 citation volume=252 citation pages=726731

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