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Analysis of mammalian alcohol dehydrogenase 5 (ADH5): Characterisation of rat ADH5 with comparisons to the corresponding human variant
Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics. Linköping University, The Institute of Technology. Karolinska Institute, Sweden .
Karolinska Institute, Sweden .
Karolinska Institute, Sweden .
Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics. Linköping University, The Institute of Technology.
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2013 (English)In: Chemico-Biological Interactions, ISSN 0009-2797, E-ISSN 1872-7786, Vol. 202, no 1-3, 97-103 p.Article in journal (Refereed) Published
Abstract [en]

Alcohol dehydrogenase 5 (ADH5) is a member of the mammalian alcohol dehydrogenase family of yet undefined functions. ADH5 was first identified at the DNA level in human and deer mouse. A rat alcohol dehydrogenase structure of similar type has been isolated at the cDNA level using human ADH5 as a screening probe, where the rat cDNA structure displayed several atypical properties. mRNA for rat ADH5 was found in multiple tissues, especially in the kidney. In vitro translation experiments indicated that rat ADH5 is expressed as efficiently as ADH1 and furthermore, rat ADH5 was readily expressed in COS cells fused to Green Fluorescent Protein. However, no soluble ADH5 protein could be heterologously expressed in Escherichia coil cells with expression systems successfully used for other mammalian ADHs, including fused to glutathione-S-transferase. Molecular modelling of the enzyme indicated that the protein does not fold in a productive way, which can be the explanation why no stable and active ADH5 has been isolated. These results indicate that ADH5, while readily expressed at the mRNA level, does not behave similarly to other mammalian ADHs investigated. The results, in vitro and in silico, suggest an unstable ADH5 structure, which can explain for why no active and stable protein can be isolated. Further possibilities are conceivable: the ADH5 protein may have to interact with a stabiliser, or the gene is actually a pseudogene.

Place, publisher, year, edition, pages
Elsevier , 2013. Vol. 202, no 1-3, 97-103 p.
Keyword [en]
Alcohol dehydrogenase, ADH classes, Enzyme family, Molecular modelling, Protein expression
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:liu:diva-93267DOI: 10.1016/j.cbi.2012.11.002ISI: 000317539500013OAI: oai:DiVA.org:liu-93267DiVA: diva2:623746
Note

Funding Agencies|Karolinska Institutet||Linkoping University||SeRC (Swedish eScience Research Centre)||

Available from: 2013-05-28 Created: 2013-05-28 Last updated: 2017-12-06

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