ArticleInternational journal of molecular sciences2023
Structural and Biochemical Investigation of Selected Pathogenic Mutants of the Human Dihydrolipoamide Dehydrogenase.
Eszter Szabo, Eva Nemes-Nikodem, Krisztina Rubina Vass, Zsofia Zambo, Eszter Zrupko, Beata Torocsik, Oliver Ozohanics, Balint Nagy, Attila Ambrus
Open access · goldAbstract read
In one paragraphArticle in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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What it found
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5 · Who and what moneyAuthors and funding
9 authors at 1 institution in 1 country.
Eszter SzaboDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 37-47 Tuzolto St., 1094 Budapest, Hungary.
Eva Nemes-NikodemDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 37-47 Tuzolto St., 1094 Budapest, Hungary.
Krisztina Rubina VassDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 37-47 Tuzolto St., 1094 Budapest, Hungary.
Zsofia ZamboDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 37-47 Tuzolto St., 1094 Budapest, Hungary.
Eszter ZrupkoDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 37-47 Tuzolto St., 1094 Budapest, Hungary.
Beata TorocsikDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 37-47 Tuzolto St., 1094 Budapest, Hungary.
Oliver OzohanicsDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 37-47 Tuzolto St., 1094 Budapest, Hungary.ORCID 0000-0002-2705-9921 Balint NagyDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 37-47 Tuzolto St., 1094 Budapest, Hungary.ORCID 0000-0003-3669-7041 Attila AmbrusDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, 37-47 Tuzolto St., 1094 Budapest, Hungary.ORCID 0000-0001-6014-3175 Semmelweis University · HU
Funding
Helmholtz Zentrum Berlin/CALIPSO MX-212-00269-STHungarian Brain Research program 2 2017-1.2.1-NKP-2017-00002Hungarian Scientific Research Fund OTKA grant 143627Ministry of Innovation and Technology of Hungary TKP2021-EGA-25New National Excellence Program of the Ministry of Innovation and Technology of Hungary ÚNKP-19-3-III-SE-17Semmelweis University STIA-OTKA-2021
6 · The paper itselfAbstract
Clinically relevant disease-causing variants of the human dihydrolipoamide dehydrogenase (hLADH, hE3), a common component of the mitochondrial α-keto acid dehydrogenase complexes, were characterized using a multipronged approach to unravel the molecular pathomechanisms that underlie hLADH deficiency. The G101del and M326V substitutions both reduced the protein stability and triggered the disassembly of the functional/obligate hLADH homodimer and significant FAD losses, which altogether eventually manifested in a virtually undetectable catalytic activity in both cases. The I12T-hLADH variant proved also to be quite unstable, but managed to retain the dimeric enzyme form; the LADH activity, both in the
Indexed as
Dihydrolipoamide Dehydrogenase3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)HumansProtein Conformation3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)Dihydrolipoamide Dehydrogenasealpha-keto acid dehydrogenase complexesdisease-causing mutationlipoamide dehydrogenasereactive oxygen speciesX-ray crystallography
Identifiers
PMID37446004
PMCPMC10341545
OpenAlexW4382726917
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