Linked Life Data

17074428

Source:http://linkedlifedata.com/resource/pubmed/id/17074428

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-2-2
pubmed:abstractText
In a previous work, we presented evidence for the presence of a protein encoded by At5g50600 in oil bodies (OBs) from Arabidopsis thaliana [P. Jolivet, E. Roux, S. D'Andrea, M. Davanture, L. Negroni, M. Zivy, T. Chardot, Protein composition of oil bodies in Arabidopsis thaliana ecotype WS, Plant Physiol. Biochem. 42 (2004) 501-509]. Using specific antibodies and proteomic techniques, we presently confirm the existence of this protein, which is a member of the short-chain steroid dehydrogenase reductase superfamily. We have measured its activity toward various steroids (cholesterol, dehydroepiandrosterone, cortisol, corticosterone, estradiol, estrone) and NAD(P)(H), either within purified OBs or as a purified bacterially expressed chimera. Both enzymatic systems (OBs purified from A. thaliana seeds as well as the chimeric enzyme) exhibited hydroxysteroid dehydrogenase (HSD) activity toward estradiol (17beta-hydroxysteroid) with NAD+ or NADP+, NADP+ being the preferred cofactor. Low levels of activity were observed with cortisol or corticosterone (11beta-hydroxysteroids), but neither cholesterol nor DHEA (3beta-hydroxysteroids) were substrates, whatever the cofactor used. Similar activity profiles were found for both enzyme sources. Purified OBs were found to be also able to catalyze estrone reduction (17beta-ketosteroid reductase activity) with NADPH. The enzyme occurring in A. thaliana OBs can be classified as a NADP+-dependent 11beta-,17beta-hydroxysteroid dehydrogenase/17beta-ketosteroid reductase. This enzyme probably corresponds to AtHSD1, which is encoded by At5g50600. However, its physiological role and substrates still remain to be determined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
89
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
222-9
pubmed:meshHeading
pubmed-meshheading:17074428-17-Hydroxysteroid Dehydrogenases, pubmed-meshheading:17074428-Amino Acid Sequence, pubmed-meshheading:17074428-Arabidopsis, pubmed-meshheading:17074428-Arabidopsis Proteins, pubmed-meshheading:17074428-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:17074428-Estradiol, pubmed-meshheading:17074428-Fatty Acid Synthetase Complex, pubmed-meshheading:17074428-Kinetics, pubmed-meshheading:17074428-Molecular Sequence Data, pubmed-meshheading:17074428-NADH, NADPH Oxidoreductases, pubmed-meshheading:17074428-NADP, pubmed-meshheading:17074428-Oxidation-Reduction, pubmed-meshheading:17074428-Phylogeny, pubmed-meshheading:17074428-Plant Oils, pubmed-meshheading:17074428-Recombinant Proteins, pubmed-meshheading:17074428-Seeds, pubmed-meshheading:17074428-Sequence Alignment, pubmed-meshheading:17074428-Substrate Specificity
pubmed:year
2007
pubmed:articleTitle
At5g50600 encodes a member of the short-chain dehydrogenase reductase superfamily with 11beta- and 17beta-hydroxysteroid dehydrogenase activities associated with Arabidopsis thaliana seed oil bodies.
pubmed:affiliation
Institut National de la Recherche Agronomique, UMR Chimie Biologique, CBAI INRA INA PG, BP1, F-78850 Thiverval Grignon, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't