| pubmed-article:8594196 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8594196 | lifeskim:mentions | umls-concept:C0038179 | lld:lifeskim |
| pubmed-article:8594196 | lifeskim:mentions | umls-concept:C0315260 | lld:lifeskim |
| pubmed-article:8594196 | lifeskim:mentions | umls-concept:C0017398 | lld:lifeskim |
| pubmed-article:8594196 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:8594196 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:8594196 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:8594196 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:8594196 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8594196 | pubmed:dateCreated | 1996-4-11 | lld:pubmed |
| pubmed-article:8594196 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8594196 | pubmed:abstractText | A 14.3 kb DNA fragment from Klebsiella oxytoca M5a1 has been cloned and shown to provide Escherichia coli with the capacity for growth on alpha- and beta-cyclodextrins. This fragment is located immediately upstream of the previously identified cgt gene coding for cyclodextrin glycosyltransferase. It contains ten genes (cym) organised in two divergently oriented clusters separated by a non-coding region of 419 bp. Four of the genes code for products homologous to the maltose and linear maltodextrin uptake system, another one for a putative cytoplasmic cyclodextrinase. The cym genes of K. oxytoca are distinct and different from the mal genes; cym mutations do not affect maltose catabolism. On the other hand, whereas mutations in the maltose/maltodextrin-uptake genes do not influence cyclodextrin metabolism, a mutation inactivating the malPQ genes coding for maltodextrin phosphorylase and amylomaltase does. Cyclodextrin catabolism is independent of the presence of a functional cyclodextrin glycosyltransferase but degradation of starch and gamma-cyclodextrins requires the activity of this enzyme. The results indicate the existence of a novel starch degradation pathway which involves the extracellular conversion of starch into cyclodextrins by cyclodextrin glycosyltransferase, uptake of the cyclodextrins by a specific uptake system and intracellular linearisation by a cyclodextrinase. The malto-oligosaccharides produced are then channelled into the maltodextrin-degradation route involving the activity of maltodextrin phosphorylase and amylomaltase. | lld:pubmed |
| pubmed-article:8594196 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8594196 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8594196 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8594196 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8594196 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8594196 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8594196 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8594196 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:8594196 | pubmed:author | pubmed-author:DoveP WPW | lld:pubmed |
| pubmed-article:8594196 | pubmed:author | pubmed-author:FiedlerGG | lld:pubmed |
| pubmed-article:8594196 | pubmed:author | pubmed-author:PajatschMM | lld:pubmed |
| pubmed-article:8594196 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8594196 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:8594196 | pubmed:volume | 256 | lld:pubmed |
| pubmed-article:8594196 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8594196 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8594196 | pubmed:pagination | 279-91 | lld:pubmed |
| pubmed-article:8594196 | pubmed:dateRevised | 2000-12-18 | lld:pubmed |
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| pubmed-article:8594196 | pubmed:meshHeading | pubmed-meshheading:8594196-... | lld:pubmed |
| pubmed-article:8594196 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8594196 | pubmed:articleTitle | Genetics of a novel starch utilisation pathway present in Klebsiella oxytoca. | lld:pubmed |
| pubmed-article:8594196 | pubmed:affiliation | Lehrstuhl für Mikrobiologie der Universität München, Munich, Germany | lld:pubmed |
| pubmed-article:8594196 | pubmed:publicationType | Journal Article | lld:pubmed |
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