| pubmed-article:3086094 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3086094 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
| pubmed-article:3086094 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:3086094 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:3086094 | lifeskim:mentions | umls-concept:C0025516 | lld:lifeskim |
| pubmed-article:3086094 | lifeskim:mentions | umls-concept:C0025519 | lld:lifeskim |
| pubmed-article:3086094 | lifeskim:mentions | umls-concept:C0040005 | lld:lifeskim |
| pubmed-article:3086094 | lifeskim:mentions | umls-concept:C0150543 | lld:lifeskim |
| pubmed-article:3086094 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:3086094 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:3086094 | pubmed:dateCreated | 1986-7-18 | lld:pubmed |
| pubmed-article:3086094 | pubmed:abstractText | L-Threonine catabolism by Saccharomyces cerevisiae was studied to determine the role of glycolytic bypath as a detoxyfication system of 2-oxoaldehyde (methylglyoxal) formed from L-threonine catabolism. During the growth on L-threonine as a sole source of nitrogen, a large amount of aminoacetone was accumulated in the culture. The enzymatic analyses indicated that L-threonine was converted into either acetaldehyde and glycine by threonine aldolase or 2-aminoacetoacetate by NAD-dependent threonine dehydrogenase. Glycine formed was condensed with acetyl-CoA by aminoacetone synthase to form 2-aminoacetoacetate, a labile compound spontaneously decarboxylated into aminoacetone. The enzyme activities of the glycolytic bypath of the cells grown on L-threonine were considerably higher than those of the cells grown on ammonium sulfate as a nitrogen source. The result indicated the possible role of glycolytic bypath as a detoxification system of methylglyoxal formed from L-threonine catabolism. | lld:pubmed |
| pubmed-article:3086094 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3086094 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3086094 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3086094 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3086094 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3086094 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3086094 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3086094 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3086094 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3086094 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3086094 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3086094 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3086094 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3086094 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:3086094 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:3086094 | pubmed:author | pubmed-author:InoueYY | lld:pubmed |
| pubmed-article:3086094 | pubmed:author | pubmed-author:WatanabeKK | lld:pubmed |
| pubmed-article:3086094 | pubmed:author | pubmed-author:FukudaYY | lld:pubmed |
| pubmed-article:3086094 | pubmed:author | pubmed-author:KimuraAA | lld:pubmed |
| pubmed-article:3086094 | pubmed:author | pubmed-author:MurataKK | lld:pubmed |
| pubmed-article:3086094 | pubmed:author | pubmed-author:ShimosakaMM | lld:pubmed |
| pubmed-article:3086094 | pubmed:author | pubmed-author:SaikusaTT | lld:pubmed |
| pubmed-article:3086094 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3086094 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:3086094 | pubmed:volume | 157 | lld:pubmed |
| pubmed-article:3086094 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3086094 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3086094 | pubmed:pagination | 297-301 | lld:pubmed |
| pubmed-article:3086094 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:meshHeading | pubmed-meshheading:3086094-... | lld:pubmed |
| pubmed-article:3086094 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3086094 | pubmed:articleTitle | Metabolism of 2-oxoaldehydes in yeasts. Possible role of glycolytic bypath as a detoxification system in L-threonine catabolism by Saccharomyces cerevisiae. | lld:pubmed |
| pubmed-article:3086094 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3086094 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:856665 | entrezgene:pubmed | pubmed-article:3086094 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3086094 | lld:pubmed |
