| pubmed-article:11359613 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11359613 | lifeskim:mentions | umls-concept:C0162741 | lld:lifeskim |
| pubmed-article:11359613 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:11359613 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:11359613 | lifeskim:mentions | umls-concept:C1157783 | lld:lifeskim |
| pubmed-article:11359613 | lifeskim:mentions | umls-concept:C1522225 | lld:lifeskim |
| pubmed-article:11359613 | lifeskim:mentions | umls-concept:C1511545 | lld:lifeskim |
| pubmed-article:11359613 | lifeskim:mentions | umls-concept:C0047738 | lld:lifeskim |
| pubmed-article:11359613 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:11359613 | pubmed:dateCreated | 2001-5-21 | lld:pubmed |
| pubmed-article:11359613 | pubmed:abstractText | Disproportionating enzyme (D-enzyme) is a plastidial alpha-1,4-glucanotransferase but its role in starch metabolism is unclear. Using a reverse genetics approach we have isolated a mutant of Arabidopsis thaliana in which the gene encoding this enzyme (DPE1) is disrupted by a T-DNA insertion. While D-enzyme activity is eliminated in the homozygous dpe1-1 mutant, changes in activities of other enzymes of starch metabolism are relatively small. During the diurnal cycle, the amount of leaf starch is higher in dpe1-1 than in wild type and the amylose to amylopectin ratio is increased, but amylopectin structure is unaltered. The amounts of starch synthesised and degraded are lower in dpe1-1 than in wild type. However, the lower amount of starch synthesised and the higher proportion of amylose are both eliminated when plants are completely de-starched by a period of prolonged darkness prior to the light period. During starch degradation, a large accumulation of malto-oligosaccharides occurs in dpe1-1 but not in wild type. These data show that D-enzyme is required for malto-oligosaccharide metabolism during starch degradation. The slower rate of starch degradation in dpe1-1 suggests that malto-oligosaccharides affect an enzyme that attacks the starch granule, or that D-enzyme itself can act directly on starch. The effects on starch synthesis and composition in dpe1-1 under normal diurnal conditions are probably a consequence of metabolism at the start of the light period, of the high levels of malto-oligosaccharides generated during the dark period. We conclude that the primary function of D-enzyme is in starch degradation. | lld:pubmed |
| pubmed-article:11359613 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11359613 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11359613 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11359613 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11359613 | pubmed:issn | 0960-7412 | lld:pubmed |
| pubmed-article:11359613 | pubmed:author | pubmed-author:SmithA MAM | lld:pubmed |
| pubmed-article:11359613 | pubmed:author | pubmed-author:SmithS MSM | lld:pubmed |
| pubmed-article:11359613 | pubmed:author | pubmed-author:TakagiMM | lld:pubmed |
| pubmed-article:11359613 | pubmed:author | pubmed-author:ZeemanS CSC | lld:pubmed |
| pubmed-article:11359613 | pubmed:author | pubmed-author:CritchleyJ... | lld:pubmed |
| pubmed-article:11359613 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11359613 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:11359613 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11359613 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11359613 | pubmed:pagination | 89-100 | lld:pubmed |
| pubmed-article:11359613 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11359613 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11359613 | pubmed:articleTitle | A critical role for disproportionating enzyme in starch breakdown is revealed by a knock-out mutation in Arabidopsis. | lld:pubmed |
| pubmed-article:11359613 | pubmed:affiliation | Institute of Cell and Molecular Biology, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JH, UK. | lld:pubmed |
| pubmed-article:11359613 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11359613 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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