pubmed-article:17562315 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17562315 | lifeskim:mentions | umls-concept:C0282528 | lld:lifeskim |
pubmed-article:17562315 | lifeskim:mentions | umls-concept:C0031673 | lld:lifeskim |
pubmed-article:17562315 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
pubmed-article:17562315 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:17562315 | lifeskim:mentions | umls-concept:C1157377 | lld:lifeskim |
pubmed-article:17562315 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:17562315 | lifeskim:mentions | umls-concept:C1261552 | lld:lifeskim |
pubmed-article:17562315 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
pubmed-article:17562315 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:17562315 | pubmed:dateCreated | 2007-6-12 | lld:pubmed |
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pubmed-article:17562315 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17562315 | pubmed:abstractText | Ether phospholipids are essential constituents of eukaryotic cell membranes. Rhizomelic chondrodysplasia punctata type 3 is a severe peroxisomal disorder caused by inborn deficiency of alkyldihydroxyacetonephosphate synthase (ADPS). The enzyme carries out the most characteristic step in ether phospholipid biosynthesis: formation of the ether bond. The crystal structure of ADPS from Dictyostelium discoideum shows a fatty-alcohol molecule bound in a narrow hydrophobic tunnel, specific for aliphatic chains of 16 carbons. Access to the tunnel is controlled by a flexible loop and a gating helix at the protein-membrane interface. Structural and mutagenesis investigations identify a cluster of hydrophilic catalytic residues, including an essential tyrosine, possibly involved in substrate proton abstraction, and the arginine that is mutated in ADPS-deficient patients. We propose that ether bond formation might be orchestrated through a covalent imine intermediate with the flavin, accounting for the noncanonical employment of a flavin cofactor in a nonredox reaction. | lld:pubmed |
pubmed-article:17562315 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17562315 | pubmed:language | eng | lld:pubmed |
pubmed-article:17562315 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17562315 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17562315 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17562315 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17562315 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17562315 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17562315 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17562315 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17562315 | pubmed:month | Jun | lld:pubmed |
pubmed-article:17562315 | pubmed:issn | 0969-2126 | lld:pubmed |
pubmed-article:17562315 | pubmed:author | pubmed-author:MatteviAndrea... | lld:pubmed |
pubmed-article:17562315 | pubmed:author | pubmed-author:RazetoAdeliaA | lld:pubmed |
pubmed-article:17562315 | pubmed:author | pubmed-author:AlivertiAless... | lld:pubmed |
pubmed-article:17562315 | pubmed:author | pubmed-author:PandiniVittor... | lld:pubmed |
pubmed-article:17562315 | pubmed:author | pubmed-author:CodaAlessandr... | lld:pubmed |
pubmed-article:17562315 | pubmed:author | pubmed-author:MattiroliFran... | lld:pubmed |
pubmed-article:17562315 | pubmed:author | pubmed-author:CarpanelliEle... | lld:pubmed |
pubmed-article:17562315 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17562315 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:17562315 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17562315 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17562315 | pubmed:pagination | 683-92 | lld:pubmed |
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pubmed-article:17562315 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17562315 | pubmed:articleTitle | The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder. | lld:pubmed |
pubmed-article:17562315 | pubmed:affiliation | Dipartimento di Genetica e Microbiologia, Università di Pavia, via Ferrata 1, 27100 Pavia, Italy. | lld:pubmed |
pubmed-article:17562315 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17562315 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:8625550 | entrezgene:pubmed | pubmed-article:17562315 | lld:entrezgene |
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