| pubmed-article:172488 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:172488 | lifeskim:mentions | umls-concept:C0317724 | lld:lifeskim |
| pubmed-article:172488 | lifeskim:mentions | umls-concept:C0059017 | lld:lifeskim |
| pubmed-article:172488 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:172488 | lifeskim:mentions | umls-concept:C0301630 | lld:lifeskim |
| pubmed-article:172488 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:172488 | pubmed:dateCreated | 1976-2-20 | lld:pubmed |
| pubmed-article:172488 | pubmed:abstractText | In Peptostreptococcus elsdenii, a three-component flavoprotein electron transfer system catalyzes the oxidation of lactate and the reduction of crotonyl-coenzyme A (CoA). Spectral evidence showed that D-lactate dehydrogenase, when reduced by D-lactate, was able to reduce butyryl-CoA dehydrogenase, but only in the presence of the electron-transferring flavoprotein. Reduced nicotinamide adenine dinucleotide could replace reduced D-lactate dehydrogenase. A reconstituted system, containing the three partially purified enzymes, excess D-lactate, and a limiting amount of crotonyl-CoA, reduced the crotonyl-CoA to butyryl-CoA, but only if all components were present. The electron-transferring flavoprotein activity, purified 22-fold, was separated into two major flavoprotein components, A and B, after polyacrylamide gel electrophoresis. Elution of the proteins and subsequent kinetic assays of the eluates showed that component B catalyzes the reduction of butyryl-CoA dehydrogenase by reduced D-lactate dehydrogenase, whereas component A does not. Both A and B catalyzed the reduction of butyryl-CoA dehydrogenase by reduced nicotinamide adenine dinucleotide. The results suggest that the D-lactate dehydrogenase-dependent reduction involves a heretofore unrecognized component of the electron-transferring protein group which may utilize an unusual flavin, 6-hydroxy-7,8-dimethyl-10-(ribityl-5'-adenosine diphosphate)-isoalloxazine. | lld:pubmed |
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| pubmed-article:172488 | pubmed:language | eng | lld:pubmed |
| pubmed-article:172488 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:172488 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:172488 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:172488 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:172488 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:172488 | pubmed:author | pubmed-author:WoodW AWA | lld:pubmed |
| pubmed-article:172488 | pubmed:author | pubmed-author:BrockmanH LHL | lld:pubmed |
| pubmed-article:172488 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:172488 | pubmed:volume | 124 | lld:pubmed |
| pubmed-article:172488 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:172488 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:172488 | pubmed:pagination | 1447-53 | lld:pubmed |
| pubmed-article:172488 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:172488 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:172488 | pubmed:articleTitle | Electron-transferring flavoprotein of Peptostreptococcus elsdenii that functions in the reduction of acrylyl-coenzyme A. | lld:pubmed |
| pubmed-article:172488 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:172488 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:172488 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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