| pubmed-article:8889583 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C0031485 | lld:lifeskim |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C0031456 | lld:lifeskim |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C1609982 | lld:lifeskim |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C0243102 | lld:lifeskim |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:8889583 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:8889583 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8889583 | pubmed:dateCreated | 1997-1-23 | lld:pubmed |
| pubmed-article:8889583 | pubmed:abstractText | We have used three complementary in vitro systems to express the human phenylalanine hydroxylase (PAH) gene at high levels. Recombinant PAH was expressed in Escherichia coli (as a fusion protein), in human kidney cells and in a cell-free in vitro transcription-translation system. These systems were used to characterize a novel kinetic variant form (D143G) of the enzyme. The recombinant D143G mutant enzyme had the same physicochemical properties as the wild-type PAH and was stable when expressed in eukaryotic cells. Enzyme activity studies of the D143G mutant enzyme, produced in the three expression systems, revealed a kinetic variant form with reduced affinity for L-Phe (about 2.4-fold increase in the S0.5 value) as well as reduced affinity for tetrahydrobiopterin (BH4) (about 2-fold increase in the apparent Km). At standard assay conditions (1 mM L-Phe, t5 microM BH4) the residual activity of the mutant enzyme was high and variable (52%, 33%, and 102%) when analysed in the three different systems. The high residual activities of the mutant enzyme obtained at these conditions were not in agreement with the classical PKU phenotype found in a patient compound heterozygous for the termination mutation G272X and the novel D143G mutation. However, when the D143G mutant enzyme was assayed at lower concentrations of L-Phe (100-300 microM) and BH4 (10 microM) the residual activities were compatible with severely reduced hydroxylation of L-Phe and the classical PKU phenotype. | lld:pubmed |
| pubmed-article:8889583 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8889583 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8889583 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8889583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8889583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8889583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8889583 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8889583 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8889583 | pubmed:issn | 1059-7794 | lld:pubmed |
| pubmed-article:8889583 | pubmed:author | pubmed-author:FlatmarkTT | lld:pubmed |
| pubmed-article:8889583 | pubmed:author | pubmed-author:ApoldJJ | lld:pubmed |
| pubmed-article:8889583 | pubmed:author | pubmed-author:MartínezAA | lld:pubmed |
| pubmed-article:8889583 | pubmed:author | pubmed-author:EikenH GHG | lld:pubmed |
| pubmed-article:8889583 | pubmed:author | pubmed-author:KnappskogP... | lld:pubmed |
| pubmed-article:8889583 | pubmed:author | pubmed-author:BrulandOO | lld:pubmed |
| pubmed-article:8889583 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8889583 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:8889583 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8889583 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8889583 | pubmed:pagination | 236-46 | lld:pubmed |
| pubmed-article:8889583 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:meshHeading | pubmed-meshheading:8889583-... | lld:pubmed |
| pubmed-article:8889583 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8889583 | pubmed:articleTitle | PKU mutation (D143G) associated with an apparent high residual enzyme activity: expression of a kinetic variant form of phenylalanine hydroxylase in three different systems. | lld:pubmed |
| pubmed-article:8889583 | pubmed:affiliation | Department of Medical Genetics, Haukeland Hospital, University of Bergen, Norway. | lld:pubmed |
| pubmed-article:8889583 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8889583 | pubmed:publicationType | Case Reports | lld:pubmed |
| pubmed-article:8889583 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5053 | entrezgene:pubmed | pubmed-article:8889583 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8889583 | lld:pubmed |
