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The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

Persson, B. and Kallberg, Y. and Bray, J.E. and Bruford, E. and Dellaporta, S.L. and Favia, A.D. and Duarte, R.G. and Jörnvall, H. and Kavanagh, K.L. and Kedishvili, N. and Kisiela, M. and Maser, E. and Mindnich, R. and Orchard, S. and Penning, T.M. and Thornton, Janet M. and Adamski, J. and Oppermann, U . (2009) The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative. Chemico-Biological Interactions 178 (1-3), pp. 94-98. ISSN 1872-7786.

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Official URL: http://dx.doi.org/10.1016/j.cbi.2008.10.040

Abstract

Short-chain dehydrogenases/reductases (SDR) constitute one of the largest enzyme superfamilies with presently over 46,000 members. In phylogenetic comparisons, members of this superfamily show early divergence where the majority have only low pairwise sequence identity, although sharing common structural properties. The SDR enzymes are present in virtually all genomes investigated, and in humans over 70 SDR genes have been identified. In humans, these enzymes are involved in the metabolism of a large variety of compounds, including steroid hormones, prostaglandins, retinoids, lipids and xenobiotics. It is now clear that SDRs represent one of the oldest protein families and contribute to essential functions and interactions of all forms of life. As this field continues to grow rapidly, a systematic nomenclature is essential for future annotation and reference purposes. A functional subdivision of the SDR superfamily into at least 200 SDR families based upon hidden Markov models forms a suitable foundation for such a nomenclature system, which we present in this paper using human SDRs as examples.

Item Type: Article
Keyword(s) / Subject(s): SDR, enzymes, nomenclature, bioinformatics, hidden Markov models
School or Research Centre: Birkbeck Schools and Research Centres > School of Science > Biological Sciences
Depositing User: Administrator
Date Deposited: 04 Aug 2010 14:09
Last Modified: 17 Apr 2013 12:17
URI: http://eprints.bbk.ac.uk/id/eprint/1126

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