| pubmed-article:9671268 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9671268 | lifeskim:mentions | umls-concept:C0037047 | lld:lifeskim |
| pubmed-article:9671268 | lifeskim:mentions | umls-concept:C1556094 | lld:lifeskim |
| pubmed-article:9671268 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:9671268 | lifeskim:mentions | umls-concept:C0009228 | lld:lifeskim |
| pubmed-article:9671268 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
| pubmed-article:9671268 | lifeskim:mentions | umls-concept:C1538557 | lld:lifeskim |
| pubmed-article:9671268 | lifeskim:mentions | umls-concept:C0450254 | lld:lifeskim |
| pubmed-article:9671268 | lifeskim:mentions | umls-concept:C0075444 | lld:lifeskim |
| pubmed-article:9671268 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9671268 | pubmed:dateCreated | 1998-9-17 | lld:pubmed |
| pubmed-article:9671268 | pubmed:abstractText | Succinyl-CoA:3-ketoacid CoA transferase (SCOT; EC 2.8.3.5; locus symbol OXCT) is the key enzyme of ketone body utilization. Hereditary SCOT deficiency (MIM 245050) causes episodes of severe ketoacidosis. We developed a transient expression system for mutant SCOT cDNAs, using immortalized SCOT-deficient fibroblasts. This paper describes and characterizes three missense mutations in two SCOT-deficient siblings from Japan. They are genetic compounds who inherited the mutation C456F (c1367 G-->T) from their mother. Their paternal allele contains two mutations in cis, T58M (c173 C-->T) and V133E (c398T-->A). Expression of SCOT cDNAs containing either V133E or C456F produces no detectable SCOT activity, whereas T58M is functionally neutral. T58M is a rare sequence variant not detected in 100 control Japanese alleles. In fibroblasts from the proband (GS02), in whom immunoblot demonstrated no detectable SCOT peptide, we measured an apparent residual SCOT activity of 20-35%. We hypothesize that the high residual SCOT activity in homogenates may be an artifact caused by use of the substrate, acetoacetyl-CoA by other enzymes. Expression of mutant SCOT cDNAs more accurately reflects the residual activity of SCOT than do currently available assays in cell or tissue homogenates. | lld:pubmed |
| pubmed-article:9671268 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9671268 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9671268 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9671268 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9671268 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9671268 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9671268 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9671268 | pubmed:issn | 1059-7794 | lld:pubmed |
| pubmed-article:9671268 | pubmed:author | pubmed-author:WatanabeHH | lld:pubmed |
| pubmed-article:9671268 | pubmed:author | pubmed-author:KondoNN | lld:pubmed |
| pubmed-article:9671268 | pubmed:author | pubmed-author:HirayamaKK | lld:pubmed |
| pubmed-article:9671268 | pubmed:author | pubmed-author:MitchellG AGA | lld:pubmed |
| pubmed-article:9671268 | pubmed:author | pubmed-author:FukaoTT | lld:pubmed |
| pubmed-article:9671268 | pubmed:author | pubmed-author:ShintakuHH | lld:pubmed |
| pubmed-article:9671268 | pubmed:author | pubmed-author:SongX QXQ | lld:pubmed |
| pubmed-article:9671268 | pubmed:author | pubmed-author:Kassovska-Bra... | lld:pubmed |
| pubmed-article:9671268 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9671268 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:9671268 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9671268 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9671268 | pubmed:pagination | 83-8 | lld:pubmed |
| pubmed-article:9671268 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:meshHeading | pubmed-meshheading:9671268-... | lld:pubmed |
| pubmed-article:9671268 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9671268 | pubmed:articleTitle | Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency: two pathogenic mutations, V133E and C456F, in Japanese siblings. | lld:pubmed |
| pubmed-article:9671268 | pubmed:affiliation | Department of Pediatrics, Gifu University School of Medicine, Japan. | lld:pubmed |
| pubmed-article:9671268 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9671268 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| literatureCitation:4003_967... | literatureCitation:pubmed | pubmed-article:9671268 | lld:drugbank |
| entrez-gene:5019 | entrezgene:pubmed | pubmed-article:9671268 | lld:entrezgene |
