β-Ureidopropionase deficiency due to novel and rare UPB1 mutations affecting pre-mRNA splicing and protein structural integrity and catalytic activity

Autor: Doreen Dobritzsch, Judith Meijer, Rutger Meinsma, Dirk Maurer, Ardeshir A. Monavari, Anders Gummesson, Annika Reims, Jorge A. Cayuela, Natalia Kuklina, Jean-François Benoist, Laurence Perrin, Birgit Assmann, Georg F. Hoffmann, Jörgen Bierau, Angela M. Kaindl, André B.P. van Kuilenburg

Publikováno v: Molecular genetics and metabolism, 136(3), 177-185. Academic Press Inc.
Molecular Genetics and Metabolism, 136(3), 177-185. Academic Press
Molecular Genetics and Metabolism, 136(3), 177-185. Academic Press Inc.

beta-Ureidopropionase is the third enzyme of the pyrimidine degradation pathway and catalyses the conversion of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyric acid to beta-alanine and beta-aminoisobutyric acid, ammonia and CO2. To date,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4548d2ad17ee7613703e5f517be70cb1
https://doi.org/10.1016/j.ymgme.2022.01.102

Genome sequencing reveals a novel genetic mechanism underlying dihydropyrimidine dehydrogenase deficiency: A novel missense variant c.1700G>A and a large intragenic inversion in DPYD spanning intron 8 to intron 12

Autor: Maja Tarailo-Graovac, André B.P. van Kuilenburg, Colin Jd Ross, Doreen Dobritzsch, Judith Meijer, Rutger Meinsma, Clara D.M. van Karnebeek, Wyeth W. Wasserman, Britt I. Drögemöller, Lida Zoetekouw, Dirk Maurer, Jerry Vockley

Publikováno v: Human mutation, 39(7), 947-953. Wiley-Liss Inc.

Dihydropyrimidine dehydrogenase (DPD) deficiency is associated with a variable clinical presentation. A family with three DPD-deficient patients presented with unusual clinical phenotypes including pregnancy-induced symptoms, transient visual impairm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ea9a34d202ab7305e63edd08dd45dbf
https://doi.org/10.1002/humu.23538

Directed Evolution of Alcohol Dehydrogenase for Improved Stereoselective Redox Transformations of 1-Phenylethane-1,2-diol and Its Corresponding Acyloin

Autor: Dirk Maurer, Thao Chu, Thilak Reddy Enugala, Mikael Widersten, Emil Hamnevik, Robin Löfgren, Doreen Dobritzsch

Publikováno v: Biochemistry. 57(7)

Laboratory evolution of alcohol dehydrogenase produced enzyme variants with improved turnover numbers with a vicinal 1,2-diol and its corresponding hydroxyketone. Crystal structure and transient kinetics analysis aids in rationalizing the new functio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bf3117f7637377e712826c9e6cb6a53
https://pubmed.ncbi.nlm.nih.gov/29384657

Severe fluoropyrimidine toxicity due to novel and rare DPYD missense mutations, deletion and genomic amplification affecting DPD activity and mRNA splicing

Autor: Raoul C.M. Hennekam, Lia Knegt, Lieke H. van Huis-Tanja, André B.P. van Kuilenburg, Roel J.W. van Kampen, Doreen Dobritzsch, Vincent O. Dezentjé, Dirk Maurer, Lida Zoetekouw, Jens Michael Hertz, Judith Meijer, Rob L. H. Jansen, Rutger Meinsma, Maartje Los

Publikováno v: BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, 1863(3), 721-730. Elsevier
Biochimica et Biophysica Acta-Molecular Basis of Disease, 1863(3), 721-730. Elsevier Science
van Kuilenburg, A B P, Meijer, J, Maurer, D, Dobritzsch, D, Meinsma, R, Los, M, Knegt, L C, Zoetekouw, L, Jansen, R L H, Dezentjé, V, van Huis-Tanja, L H, van Kampen, R J W, Hertz, J M & Hennekam, R C M 2017, ' Severe fluoropyrimidine toxicity due to novel and rare DPYD missense mutations, deletion and genomic amplification affecting DPD activity and mRNA splicing ', BBA Molecular Basis of Disease, vol. 1863, no. 3, pp. 721-730 . https://doi.org/10.1016/j.bbadis.2016.12.010

Dihydropyrimidine dehydrogenase (DPD) is the initial and rate-limiting enzyme in the catabolism of 5-fluorouracil (5FU). Genetic variations in DPD have emerged as predictive risk factors for severe fluoropyrimidine toxicity. Here, we report novel and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::003c2701657a7e36863887462c681232
https://pubmed.ncbi.nlm.nih.gov/28024938