| http://purl.uniprot.org/citations/15051722 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15051722 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15051722 | http://www.w3.org/2000/01/rdf-schema#comment | "2-Enoyl-CoA hydratase 2, a part from multifunctional enzyme type 2, hydrates trans-2-enoyl-CoA to 3-hydroxyacyl-CoA in the (3R)-hydroxy-dependent route of peroxisomal beta-oxidation of fatty acids. Unliganded and (3R)-hydroxydecanoyl coenzyme A-complexed crystal structures of 2-enoyl-CoA hydratase 2 from Candida tropicalis multifunctional enzyme type 2 were solved to 1.95- and 2.35-A resolution, respectively. 2-Enoyl-CoA hydratase 2 is a dimeric, alpha+beta protein with a novel quaternary structure. The overall structure of the two-domain subunit of eukaryotic 2-enoyl-CoA hydratase 2 resembles the homodimeric, hot dog fold structures of prokaryotic (R)-specific 2-enoyl-CoA hydratase and beta-hydroxydecanoyl thiol ester dehydrase. Importantly, though, the eukaryotic hydratase 2 has a complete hot dog fold only in its C-domain, whereas the N-domain lacks a long central alpha-helix, thus creating space for bulkier substrates in the binding pocket and explaining the observed difference in substrate preference between eukaryotic and prokaryotic enzymes. Although the N- and C-domains have an identity of <10% at the amino acid level, they share a 50% identity at the nucleotide level and fold similarly. We suggest that a subunit of 2-enoyl-CoA hydratase 2 has evolved via a gene duplication with the concomitant loss of one catalytic site. The hydrogen bonding network of the active site of 2-enoyl-CoA hydratase 2 resembles the active site geometry of mitochondrial (S)-specific 2-enoyl-CoA hydratase 1, although in a mirror image fashion. This arrangement allows the reaction to occur by similar mechanism, supported by mutagenesis and mechanistic studies, although via reciprocal stereochemistry."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m400293200"xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m400293200"xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/author | "Hiltunen J.K."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/author | "Hiltunen J.K."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/author | "Haapalainen A.M."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/author | "Haapalainen A.M."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/author | "Koski M.K."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/author | "Koski M.K."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/author | "Glumoff T."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/author | "Glumoff T."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/pages | "24666-24672"xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/pages | "24666-24672"xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/title | "A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/title | "A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2."xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15051722 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15051722 |
| http://purl.uniprot.org/citations/15051722 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15051722 |