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A hydrogen-bonding network in mammalian sorbitol dehydrogenase stabilizes the tetrameric state and is essential for the catalytic power
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID iD: 0000-0001-5257-6261
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
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2007 (English)In: Cellular and Molecular Life Sciences (CMLS), ISSN 1420-682X, E-ISSN 1420-9071, Vol. 64, no 23, p. 3129-3138Article in journal (Refereed) Published
Abstract [en]

Subunit interaction in sorbitol dehydrogenase (SDH) has been studied with in vitro and in silico methods identifying a vital hydrogen-bonding network, which is strictly conserved among mammalian SDH proteins. Mutation of one of the residues in the hydrogen-bonding network, Tyr110Phe, abolished the enzymatic activity and destabilized the protein into tetramers, dimers and monomers as judged from gel filtration experiments at different temperatures compared to only tetramers for the wild-type protein below 307 K. The determined equilibrium constants revealed a large difference in Gibbs energy (8 kJ/mol) for the tetramer stability between wild-type SDH and the mutated form Tyr110Phe SDH. The results focus on a network of coupled hydrogen bonds in wild-type SDH that uphold the protein interface, which is specific and favorable to electrostatic, van der Waals and hydrogen-bond interactions between subunits, interactions that are crucial for the catalytic power of SDH. 

Place, publisher, year, edition, pages
Springer, 2007. Vol. 64, no 23, p. 3129-3138
Keywords [en]
Alcohol dehydrogenase, hydrogen-bonding network, Gibbs energy, quaternary structure, sorbitol dehydrogenase, structural zinc
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:oru:diva-109971DOI: 10.1007/s00018-007-7318-1ISI: 000251879000011PubMedID: 17952367Scopus ID: 2-s2.0-38549169038OAI: oai:DiVA.org:oru-109971DiVA, id: diva2:1815929
Available from: 2023-11-30 Created: 2023-11-30 Last updated: 2023-12-01Bibliographically approved

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