| pubmed-article:20060505 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20060505 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:20060505 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:20060505 | lifeskim:mentions | umls-concept:C0060605 | lld:lifeskim |
| pubmed-article:20060505 | lifeskim:mentions | umls-concept:C1657244 | lld:lifeskim |
| pubmed-article:20060505 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:20060505 | pubmed:dateCreated | 2010-3-24 | lld:pubmed |
| pubmed-article:20060505 | pubmed:abstractText | FAD synthetase or ATP:FMN adenylyl transferase (FADS or FMNAT, EC 2.7.7.2) is a key enzyme in the metabolic pathway that converts riboflavin into the redox cofactor FAD. We face here the still controversial sub-cellular localization of FADS in eukaryotes. First, by western blotting experiments, we confirm the existence in rat liver of different FADS isoforms which are distinct for molecular mass and sub-cellular localization. A cross-reactive band with an apparent molecular mass of 60 kDa on SDS-PAGE is localized in the internal compartments of freshly isolated purified rat liver mitochondria. Recently we have identified two isoforms of FADS in humans, that differ for an extra-sequence of 97 amino acids at the N-terminus, present only in isoform 1 (hFADS1). The first 17 residues of hFADS1 represent a cleavable mitochondrial targeting sequence (by Target-P prediction). The recombinant hFADS1 produced in Escherichia coli showed apparent K(m) and V(max) values for FMN equal to 1.3+/-0.7 microM and 4.4+/-1.3 nmol x min(-1) x mg protein(-1), respectively, and was inhibited by FMN at concentration higher than 1.5 microM. The in vitro synthesized hFADS1, but not hFADS2, is imported into rat liver mitochondria and processed into a lower molecular mass protein product. Immunofluorescence confocal microscopy performed on BHK-21 and Caco-2 cell lines transiently expressing the two human isoforms, definitively confirmed that hFADS1, but not hFADS2, localizes in mitochondria. | lld:pubmed |
| pubmed-article:20060505 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20060505 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20060505 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20060505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20060505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20060505 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20060505 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20060505 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:20060505 | pubmed:issn | 1872-8278 | lld:pubmed |
| pubmed-article:20060505 | pubmed:author | pubmed-author:RobertiMarina... | lld:pubmed |
| pubmed-article:20060505 | pubmed:author | pubmed-author:IndiveriCesar... | lld:pubmed |
| pubmed-article:20060505 | pubmed:author | pubmed-author:BrizioCarmenC | lld:pubmed |
| pubmed-article:20060505 | pubmed:author | pubmed-author:BarileMariaM | lld:pubmed |
| pubmed-article:20060505 | pubmed:author | pubmed-author:ColellaMatild... | lld:pubmed |
| pubmed-article:20060505 | pubmed:author | pubmed-author:GiancasperoTe... | lld:pubmed |
| pubmed-article:20060505 | pubmed:author | pubmed-author:GalluccioMich... | lld:pubmed |
| pubmed-article:20060505 | pubmed:author | pubmed-author:TorchettiEnza... | lld:pubmed |
| pubmed-article:20060505 | pubmed:copyrightInfo | Copyright 2010 Mitochondria Research Society. Published by Elsevier B.V. All rights reserved. | lld:pubmed |
| pubmed-article:20060505 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20060505 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:20060505 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20060505 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20060505 | pubmed:pagination | 263-73 | lld:pubmed |
| pubmed-article:20060505 | pubmed:meshHeading | pubmed-meshheading:20060505... | lld:pubmed |
| pubmed-article:20060505 | pubmed:meshHeading | pubmed-meshheading:20060505... | lld:pubmed |
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| pubmed-article:20060505 | pubmed:meshHeading | pubmed-meshheading:20060505... | lld:pubmed |
| pubmed-article:20060505 | pubmed:meshHeading | pubmed-meshheading:20060505... | lld:pubmed |
| pubmed-article:20060505 | pubmed:meshHeading | pubmed-meshheading:20060505... | lld:pubmed |
| pubmed-article:20060505 | pubmed:meshHeading | pubmed-meshheading:20060505... | lld:pubmed |
| pubmed-article:20060505 | pubmed:meshHeading | pubmed-meshheading:20060505... | lld:pubmed |
| pubmed-article:20060505 | pubmed:meshHeading | pubmed-meshheading:20060505... | lld:pubmed |
| pubmed-article:20060505 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20060505 | pubmed:articleTitle | Mitochondrial localization of human FAD synthetase isoform 1. | lld:pubmed |
| pubmed-article:20060505 | pubmed:affiliation | Dipartimento di Biochimica e Biologia Molecolare E. Quagliariello, Università degli Studi di Bari, Via Orabona 4, I-70126 Bari, Italy. em.torchetti@biologia.uniba.it | lld:pubmed |
| pubmed-article:20060505 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20060505 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:3992 | entrezgene:pubmed | pubmed-article:20060505 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20060505 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20060505 | lld:pubmed |
