A mild phenotype of dihydropyrimidine dehydrogenase deficiency and developmental retardation associated with a missense mutation affecting cofactor binding

Sabine Weidensee; Peter Goettig; Marko Bertone; Dorothea Haas; Viktor Magdolen; Marion Kiechle; Alfons Meindl; André B. P. van Kuilenburg; Eva Gross

doi:10.1016/j.clinbiochem.2011.03.033

A mild phenotype of dihydropyrimidine dehydrogenase deficiency and developmental retardation associated with a missense mutation affecting cofactor binding

Sabine Weidensee
, Peter Goettig
, Marko Bertone
, Dorothea Haas
, Viktor Magdolen
, Marion Kiechle
, Alfons Meindl
, André B. P. van Kuilenburg
, Eva Gross

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Evaluation of a non-synonymous mutation associated with dihydropyrimidine dehydrogenase (DPD) deficiency. DPD enzyme analysis, mutation analysis and molecular dynamics simulations based on the 3D-model of DPD. 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. Like other DPD variants attenuating FAD binding, Lys63Glu should be included in screening for DPD deficiency

Original language	English
Pages (from-to)	722-724
Journal	Clinical biochemistry
Volume	44
Issue number	8-9
DOIs	https://doi.org/10.1016/j.clinbiochem.2011.03.033
Publication status	Published - 2011

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10.1016/j.clinbiochem.2011.03.033

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Weidensee, S., Goettig, P., Bertone, M., Haas, D., Magdolen, V., Kiechle, M., Meindl, A., van Kuilenburg, A. B. P., & Gross, E. (2011). A mild phenotype of dihydropyrimidine dehydrogenase deficiency and developmental retardation associated with a missense mutation affecting cofactor binding. Clinical biochemistry, 44(8-9), 722-724. https://doi.org/10.1016/j.clinbiochem.2011.03.033

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title = "A mild phenotype of dihydropyrimidine dehydrogenase deficiency and developmental retardation associated with a missense mutation affecting cofactor binding",

abstract = "Evaluation of a non-synonymous mutation associated with dihydropyrimidine dehydrogenase (DPD) deficiency. DPD enzyme analysis, mutation analysis and molecular dynamics simulations based on the 3D-model of DPD. 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. Like other DPD variants attenuating FAD binding, Lys63Glu should be included in screening for DPD deficiency",

author = "Sabine Weidensee and Peter Goettig and Marko Bertone and Dorothea Haas and Viktor Magdolen and Marion Kiechle and Alfons Meindl and \{van Kuilenburg\}, \{Andr{\'e} B. P.\} and Eva Gross",

year = "2011",

doi = "10.1016/j.clinbiochem.2011.03.033",

language = "English",

volume = "44",

pages = "722--724",

journal = "Clinical biochemistry",

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Weidensee, S, Goettig, P, Bertone, M, Haas, D, Magdolen, V, Kiechle, M, Meindl, A, van Kuilenburg, ABP & Gross, E 2011, 'A mild phenotype of dihydropyrimidine dehydrogenase deficiency and developmental retardation associated with a missense mutation affecting cofactor binding', Clinical biochemistry, vol. 44, no. 8-9, pp. 722-724. https://doi.org/10.1016/j.clinbiochem.2011.03.033

TY - JOUR

T1 - A mild phenotype of dihydropyrimidine dehydrogenase deficiency and developmental retardation associated with a missense mutation affecting cofactor binding

AU - Weidensee, Sabine

AU - Goettig, Peter

AU - Bertone, Marko

AU - Haas, Dorothea

AU - Magdolen, Viktor

AU - Kiechle, Marion

AU - Meindl, Alfons

AU - van Kuilenburg, André B. P.

AU - Gross, Eva

PY - 2011

Y1 - 2011

N2 - Evaluation of a non-synonymous mutation associated with dihydropyrimidine dehydrogenase (DPD) deficiency. DPD enzyme analysis, mutation analysis and molecular dynamics simulations based on the 3D-model of DPD. 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. Like other DPD variants attenuating FAD binding, Lys63Glu should be included in screening for DPD deficiency

AB - Evaluation of a non-synonymous mutation associated with dihydropyrimidine dehydrogenase (DPD) deficiency. DPD enzyme analysis, mutation analysis and molecular dynamics simulations based on the 3D-model of DPD. 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. Like other DPD variants attenuating FAD binding, Lys63Glu should be included in screening for DPD deficiency

U2 - 10.1016/j.clinbiochem.2011.03.033

DO - 10.1016/j.clinbiochem.2011.03.033

M3 - Article

C2 - 21420945

SN - 0009-9120

VL - 44

SP - 722

EP - 724

JO - Clinical biochemistry

JF - Clinical biochemistry

IS - 8-9

ER -

A mild phenotype of dihydropyrimidine dehydrogenase deficiency and developmental retardation associated with a missense mutation affecting cofactor binding

Abstract

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