| pubmed-article:16698902 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16698902 | lifeskim:mentions | umls-concept:C0162741 | lld:lifeskim |
| pubmed-article:16698902 | lifeskim:mentions | umls-concept:C0005194 | lld:lifeskim |
| pubmed-article:16698902 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
| pubmed-article:16698902 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:16698902 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:16698902 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:16698902 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16698902 | pubmed:dateCreated | 2006-7-7 | lld:pubmed |
| pubmed-article:16698902 | pubmed:abstractText | Nine genes of Arabidopsis (Arabidopsis thaliana) encode for beta-amylase isozymes. Six members of the family are predicted to be extrachloroplastic isozymes and three contain predicted plastid transit peptides. Among the latter, chloroplast-targeted beta-amylase (At4g17090) and thioredoxin-regulated beta-amylase (TR-BAMY; At3g23920; this work) are experimentally demonstrated to be targeted to plastids. Recombinant TR-BAMY was catalytically active only when expressed as a mature protein, i.e. with no transit peptide. Mature TR-BAMY was a monomer of 60 kD, hydrolyzing soluble starch with optimal activity between pH 6.0 and 8.0. The activity of recombinant TR-BAMY was strictly dependent on redox potential with an Em,7.0 of -302 +/- 14 mV. Thioredoxins f1, m1, and y1 of Arabidopsis were all able to mediate the reductive activation of oxidized TR-BAMY. Site-specific mutants showed that TR-BAMY oxidative inhibition depended on the formation of a disulfide bridge between Cys-32 and Cys-470. Consistent with TR-BAMY redox dependency, total beta-amylase activity in Arabidopsis chloroplasts was partially redox regulated and required reducing conditions for full activation. In Arabidopsis, TR-BAMY transcripts were detected in leaves, roots, flowers, pollen, and seeds. TR-BAMY may be the only beta-amylase of nonphotosynthetic plastids suggesting a redox regulation of starch metabolism in these organelles. In leaves, where chloroplast-targeted beta-amylase is involved in physiological degradation of starch in the dark, TR-BAMY is proposed to participate to a redox-regulated pathway of starch degradation under specific stress conditions. | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16698902 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16698902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16698902 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16698902 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:16698902 | pubmed:issn | 0032-0889 | lld:pubmed |
| pubmed-article:16698902 | pubmed:author | pubmed-author:Lo... | lld:pubmed |
| pubmed-article:16698902 | pubmed:author | pubmed-author:SparlaFrances... | lld:pubmed |
| pubmed-article:16698902 | pubmed:author | pubmed-author:PupilloPaoloP | lld:pubmed |
| pubmed-article:16698902 | pubmed:author | pubmed-author:TrostPaoloP | lld:pubmed |
| pubmed-article:16698902 | pubmed:author | pubmed-author:CostaAlexA | lld:pubmed |
| pubmed-article:16698902 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16698902 | pubmed:volume | 141 | lld:pubmed |
| pubmed-article:16698902 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16698902 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16698902 | pubmed:pagination | 840-50 | lld:pubmed |
| pubmed-article:16698902 | pubmed:dateRevised | 2010-9-16 | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:meshHeading | pubmed-meshheading:16698902... | lld:pubmed |
| pubmed-article:16698902 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16698902 | pubmed:articleTitle | Redox regulation of a novel plastid-targeted beta-amylase of Arabidopsis. | lld:pubmed |
| pubmed-article:16698902 | pubmed:affiliation | Laboratory of Molecular Plant Physiology, Department of Experimental Evolutionary Biology, University of Bologna, I-40126 Bologna, Italy. | lld:pubmed |
| pubmed-article:16698902 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16698902 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
