Linked Life Data

8328804

Source:http://linkedlifedata.com/resource/pubmed/id/8328804

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1993-8-10
pubmed:abstractText
A pathway of succinate fermentation to acetate and butanoate (butyrate) in Clostridium kluyveri has been supported by the results of 13C nuclear magnetic resonance studies of the metabolic end products of growth and the detection of dehydrogenase activities involved in the conversion of succinate to 4-hydroxybutanoate (succinic semialdehyde dehydrogenase and 4-hydroxybutanoate dehydrogenase). C. kluyveri fermented [1,4-13C]succinate primarily to [1-13C]acetate, [2-13C]acetate, and [1,4-13C]butanoate. Any pathway proposed for this metabolism must account for the reduction of a carboxyl group to a methyl group. Succinic semialdehyde dehydrogenase activity was demonstrated after separation of the crude extracts of cells grown on succinate and ethanol (succinate cells) by anaerobic nondenaturing polyacrylamide gel electrophoresis. 4-Hydroxybutanoate dehydrogenase activity in crude extracts of succinate cells was detected and characterized. Neither activity was found in cells grown on acetate and ethanol (acetate cells). Analysis of cell extracts from acetate cells and succinate cells by sodium dodecyl sulfate-polyacrylamide gel electrophoreses showed that several proteins were present in succinate cell extracts that were not present in acetate cell extracts. In addition to these changes in protein composition, less ethanol dehydrogenase and hydrogenase activity was present in the crude extracts from succinate cells than in the crude extracts from acetate cells. These data support the hypothesis that C. kluyveri uses succinate as an electron acceptor for the reducing equivalents generated from the ATP-producing oxidation of ethanol.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-13687513, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-14907713, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-15390409, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-16453537, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-16560506, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-4055746, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-5655494, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-5923901, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-6175245, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-6630146, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-6783613, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-8444151, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-860983, http://linkedlifedata.com/resource/pubmed/commentcorrection/8328804-914779
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0099-2240
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1876-82
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Dehydrogenases involved in the conversion of succinate to 4-hydroxybutanoate by Clostridium kluyveri.
pubmed:affiliation
Department of Biochemistry, University of Wisconsin, Madison 53706.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't