Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition

Autor: D. Sean Froese, Jolanta Kopec, Elzbieta Rembeza, Gustavo Arruda Bezerra, Anselm Erich Oberholzer, Terttu Suormala, Seraina Lutz, Rod Chalk, Oktawia Borkowska, Matthias R. Baumgartner, Wyatt W. Yue

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)

The human enzyme MTHFR links the folate and methionine cycles, which are essential for the biosynthesis of nucleotides and proteins. Here, the authors present the crystal structure and biochemical analysis of human MTHFR, providing molecular insights

Externí odkaz: https://doaj.org/article/81b79808dd01406c825d1806af1a047c

Functional characterization of missense mutations in severe methylenetetrahydrofolate reductase deficiency using a human expression system

Autor: D. Sean Froese, Terttu Suormala, Brian Fowler, Patricie Burda, Dorothea M. Heuberger, Matthias R. Baumgartner, Alexandra Schäfer

Publikováno v: Europe PubMed Central
Journal of inherited metabolic disease

5,10-Methylenetetrahydrofolate reductase (MTHFR) catalyzes the NADPH-dependent reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate using FAD as the cofactor. Severe MTHFR deficiency is the most common inborn error of folate metabo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfbe4030cc1d05cbc0386f210265df5f
https://doi.org/10.1007/s10545-016-9987-0

Genetic, structural, and functional analysis of mutations causing methylmalonyl-CoA epimerase deficiency

Autor: Matthias R. Baumgartner, Seraina Lutz, Patricie Burda, Brian Fowler, Wyatt W. Yue, Henry J. Bailey, Apirat Chaikuad, Terttu Suormala, Heuberger K, Céline Bürer, Krysztofinska E, D. S. Froese

Human methylmalonyl-CoA epimerase (MCEE) catalyzes the interconversion of D-methylmalonyl-CoA and L-methylmalonyl-CoA in propionate catabolism. Autosomal recessive mutations inMCEEreportedly cause methylmalonic aciduria (MMAuria) in eleven patients.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dab541ea30977de4a5d7a9b56afe485b
https://www.zora.uzh.ch/id/eprint/181019/

Splice-shifting oligonucleotide (SSO) mediated blocking of an exonic splicing enhancer (ESE) created by the prevalent c.903+469T>C MTRR mutation corrects splicing and restores enzyme activity in patient cells

Autor: Rugivan Sabaratnam, Bruno Palhais, Veronica S. Præstegaard, Henriette Skovgaard Andersen, Viktor Kožich, Patricie Burda, Thomas Koed Doktor, Seraina Lutz, Brian Fowler, Gitte Hoffmann Bruun, Terttu Suormala, Matthias R. Baumgartner, Brage S. Andresen

Publikováno v: Palhais, B, Præstegaard, V, Sabaratnam, R, Doktor, T K, Lutz, S, Burda, P, Suormala, T, Baumgartner, M, Fowler, B, Bruun, G H, Andersen, H S, Kozich, V & Andresen, B S 2015, ' Splice-shifting oligonucleotide (SSO) mediated blocking of an exonic splicing enhancer (ESE) created by the prevalent c.903+469T >C MTRR mutation corrects splicing and restores enzyme activity in patient cells ', Nucleic Acids Research, vol. 43, no. 9, pp. 4627-4639 . https://doi.org/10.1093/nar/gkv275
Nucleic acids research
Nucleic Acids Research

The prevalent c.903+469T>C mutation in MTRR causes the cblE type of homocystinuria by strengthening an SRSF1 binding site in an ESE leading to activation of a pseudoexon. We hypothesized that other splicing regulatory elements (SREs) are also critica

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc5593c4df1086ed2ec9da4f833a3270
http://doc.rero.ch/record/292780/files/gkv275.pdf

An X-linked cobalamin disorder caused by mutations in transcriptional coregulator HCFC1

Autor: Terttu Suormala, Alison Brebner, Anita M. Quintana, Jennifer L. Sloan, Tamim H. Shaikh, David S. Rosenblatt, Matthias R. Baumgartner, Elizabeth A. Geiger, Gunter Scharer, Charles P. Venditti, Curtis R. Coughlin, Una Schneck, Brian Fowler, Nathan P. Achilly, Hung-Chun Yu, Johan L.K. Van Hove, David Watkins, Irini Manoli

Publikováno v: American Journal of Human Genetics

Derivatives of vitamin B12 (cobalamin) are essential cofactors for enzymes required in intermediary metabolism. Defects in cobalamin metabolism lead to disorders characterized by the accumulation of methylmalonic acid and/or homocysteine in blood and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33376f9fb279a574075ced42c7ea8585