Clinical biochemistry · 2011
A mild phenotype of dihydropyrimidine dehydrogenase deficiency and developmental retardation associated with a missense mutation affecting cofactor binding.
Клинический случайСтатьяНазвание и аннотация: Перевод пока не подготовлен
Обработка статьи · этапы, ошибки и управление
Загрузка состояния…
Ошибки и ограничения
История · было → стало
Состояние обновляется каждые 5 секунд, пока блок открыт. Процент показывается только там, где известен объём работы. Пауза останавливает продолжение этапа; текущий запрос к источнику может завершиться.
Weidensee Sabine, Goettig Peter, Bertone Marko, Haas Dorothea, Magdolen Viktor, Kiechle Marion, Meindl Alfons, van Kuilenburg André B P, Gross Eva
Аннотация
OBJECTIVES: Evaluation of a non-synonymous mutation associated with dihydropyrimidine dehydrogenase (DPD) deficiency.
DESIGN AND METHODS: DPD enzyme analysis, mutation analysis and molecular dynamics simulations based on the 3D-model of DPD.
RESULTS: The substitution Lys63Glu is likely to affect the FAD binding pocket within the DPD protein and contributes to a near-complete DPD deficiency in a patient with developmental retardation.
CONCLUSIONS: Like other DPD variants attenuating FAD binding, Lys63Glu should be included in screening for DPD deficiency.
DESIGN AND METHODS: DPD enzyme analysis, mutation analysis and molecular dynamics simulations based on the 3D-model of DPD.
RESULTS: The substitution Lys63Glu is likely to affect the FAD binding pocket within the DPD protein and contributes to a near-complete DPD deficiency in a patient with developmental retardation.
CONCLUSIONS: Like other DPD variants attenuating FAD binding, Lys63Glu should be included in screening for DPD deficiency.