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http://purl.uniprot.org/citations/26902786http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26902786http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26902786http://www.w3.org/2000/01/rdf-schema#comment"Mitochondrial aspartate aminotransferase (mAspAT) was recognized as a moonlighting enzyme because it has not only aminotransferase activity but also a high-affinity long-chain fatty acids (LCFA) binding site. This enzyme plays a key role in amino acid metabolism, biosynthesis of kynurenic acid and transport of the LCFA. Therefore, it is important to study the structure-function relationships of human mAspAT protein. In this work, the mature form of human mAspAT was expressed to a high level in Escherichia coli periplasmic space using pET-22b vector, purified by a combination of immobilized metal-affinity chromatography and cation exchange chromatography. Optimal activity of the enzyme occurred at a temperature of 47.5ºC and a pH of 8.5. Crystals of human mAspAT were grown using the hanging-drop vapour diffusion method at 277K with 0.1 M HEPES pH 6.8 and 25%(v/v) Jeffamine(®) ED-2001 pH 6.8. The crystals diffracted to 2.99 Å and belonged to the space group P1 with the unit-cell parameters a =56.7, b = 76.1, c = 94.2 Å, α =78.0, β =85.6, γ = 78.4º. Elucidation of mAspAT structure can provide a molecular basis towards understanding catalysis mechanism and substrate binding site of enzyme."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.org/dc/terms/identifier"doi:10.5582/bst.2015.01150"xsd:string
http://purl.uniprot.org/citations/26902786http://purl.org/dc/terms/identifier"doi:10.5582/bst.2015.01150"xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/author"Chang H."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/author"Chang H."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/author"Jiang X."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/author"Jiang X."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/author"Zhou Y."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/author"Zhou Y."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/name"Biosci. Trends"xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/name"Biosci. Trends"xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/pages"79-84"xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/pages"79-84"xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/title"Recombinant expression, purification and crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/title"Recombinant expression, purification and crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase."xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/26902786http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/26902786http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26902786
http://purl.uniprot.org/citations/26902786http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26902786