The multi-protein family of sulfotransferases in plants: composition, occurrence, substrate specificity, and functions

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dc.identifier.uri http://dx.doi.org/10.15488/15
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/33
dc.contributor.author Hirschmann, Felix
dc.contributor.author Krause, Florian
dc.contributor.author Papenbrock, Jutta
dc.date.accessioned 2015-07-31T11:17:06Z
dc.date.available 2015-07-31T11:17:06Z
dc.date.issued 2014
dc.identifier.citation Hirschmann, Felix; Krause, Florian; Papenbrock, Jutta: The multi-protein family of sulfotransferases in plants: composition, occurrence, substrate specificity, and functions. In: Frontiers in Plant Science 5 (2014). DOI: http://dx.doi.org/10.3389/fpls.2014.00556
dc.description.abstract All members of the sulfotransferase (SOT, EC 2.8.2.-) protein family transfer a sulfuryl group from the donor 3’-phosphoadenosine 5’-phosphosulfate (PAPS) to an appropriate hydroxyl group of several classes of substrates. The primary structure of these enzymes is characterized by a histidine residue in the active site, defined PAPS binding sites and a longer SOT domain. Proteins with this SOT domain occur in all organisms from all three domains, usually as a multi-protein family. Arabidopsis thaliana SOTs, the best characterized SOT multi-protein family, contains 21 members. The substrates for several plant enzymes have already been identified, such as glucosinolates, brassinosteroids, jasmonates, flavonoids, and salicylic acid. Much information has been gathered on desulfoglucosinolate (dsGl) SOTs in A. thaliana. The three cytosolic dsGI SOTs show slightly different expression patterns. The recombinant proteins reveal differences in their affinity to indolic and aliphatic dsGls. Also the respective recombinant dsGl SOTs from different A. thaliana ecotypes differ in their kinetic properties. However, determinants of substrate specificity and the exact reaction mechanism still need to be clarified. Probably, the three-dimensional structures of more plant proteins need to be solved to analyze the mode of action and the responsible amino acids for substrate binding. In addition to A. thaliana, more plant species from several families need to be investigated to fully elucidate the diversity of sulfated molecules and the way of biosynthesis catalyzed by SOT enzymes. eng
dc.description.sponsorship DFG/PA/764/10-1
dc.language.iso eng eng
dc.publisher Lausanne : Frontiers Research Foundation
dc.relation.ispartofseries Frontiers in Plant Science 5 (2014)
dc.rights CC BY 4.0 Unported
dc.rights.uri http://creativecommons.org/licenses/by/4.0/
dc.subject Arabidopsis thaliana eng
dc.subject glucosinolate eng
dc.subject histidine residue eng
dc.subject phosphoadenosine 5 ‘-phosphosulfate eng
dc.subject Sulfotransferase eng
dc.subject Arabidopsis thaliana ger
dc.subject Ackerschmalwand ger
dc.subject Brassicaceae ger
dc.subject Kreuzblütengewächs ger
dc.subject Glucosinolate ger
dc.subject Senfölglycoside ger
dc.subject Histidin ger
dc.subject 3’-phosphoadenosine 5’-phosphosulfate ger
dc.subject PAPS ger
dc.subject Sulfotransferasen ger
dc.subject.classification Ackerschmalwand ger
dc.subject.classification Kreuzblütler ger
dc.subject.classification Glucosinolate ger
dc.subject.classification Histidin ger
dc.subject.classification Phosphoadenosinphosphosulfat ger
dc.subject.classification Sulfotransferasen ger
dc.subject.ddc 580 | Pflanzen (Botanik)
dc.title The multi-protein family of sulfotransferases in plants: composition, occurrence, substrate specificity, and functions eng
dc.type article
dc.type Text
dc.relation.issn 1664-462X
dc.relation.doi http://dx.doi.org/10.3389/fpls.2014.00556
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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