NDLI: Hep27, a member of the short-chain dehydrogenase/reductase family, is an NADPH-dependent dicarbonyl reductase expressed in vascular endothelial tissue

Content Provider	Springer Nature Link
Author	Shafqat, N. Shafqat, J. Eissner, G. Marschall, H. U. Tryggvason, K. Eriksson, U. Gabrielli, F. Lardy, H. Jörnvall, H. Oppermann, U.
Copyright Year	2006
Abstract	Human Hep27 was originally isolated from growth-arrested HepG2 cells and identified as a member of the superfamily of short-chain dehydrogenases/reductases (SDR). Its substrate specificity has not been determined, but a cross-species comparison suggests that it occurs in widely divergent species, such as human, Cenorhabditis elegans, Drosophila and Arabidopsis thaliana. In this study, Hep27 was expressed as a His6 fusion protein, and subjected to a substrate screen, using a compound library of SDR substrates, comprising steroids, retinoids, sugars and carbonyl compounds. Whereas no steroid dehydrogenase or retinoid activity was detected, it was found that Hep27 catalyzed the NADPH-dependent reduction of dicarbonyl compounds, like 3,4-hexanedione and 1-phenyl-1,2-propanedione with similar turnover numbers as DCXR (a mitochondrial dicarbonyl reductase/xylulose reductase). In contrast, Hep27 does not convert sugar substrates like xylulose or threose. Based on its substrate specificity and expression in endothelial tissues, it is suggested that Hep27 functions as a dicarbonyl reductase in enzymatic inactivation of reactive carbonyls, involved in covalent modification of cellular components.
Starting Page	1205
Ending Page	1213
Page Count	9
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	63
Issue Number	10
e-ISSN	14209071
Language	English
Publisher	Birkhäuser-Verlag
Publisher Date	2006-05-10
Publisher Place	Basel
Access Restriction	Subscribed
Subject Keyword	Hep27 carbonyl reductase short-chain dehydrogenase/reductase dicarbonyl compounds Life Sciences Biomedicine general Biochemistry Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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