Literature DB >> 19027726

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

Bengt Persson1, Yvonne Kallberg, James E Bray, Elspeth Bruford, Stephen L Dellaporta, Angelo D Favia, Roser Gonzalez Duarte, Hans Jörnvall, Kathryn L Kavanagh, Natalia Kedishvili, Michael Kisiela, Edmund Maser, Rebekka Mindnich, Sandra Orchard, Trevor M Penning, Janet M Thornton, Jerzy Adamski, Udo Oppermann.   

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.

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Year:  2008        PMID: 19027726      PMCID: PMC2896744          DOI: 10.1016/j.cbi.2008.10.040

Source DB:  PubMed          Journal:  Chem Biol Interact        ISSN: 0009-2797            Impact factor:   5.192


  22 in total

Review 1.  Forms and functions of human SDR enzymes.

Authors:  U C Oppermann; C Filling; H Jörnvall
Journal:  Chem Biol Interact       Date:  2001-01-30       Impact factor: 5.192

2.  The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases.

Authors:  D K Stammers; J Ren; K Leslie; C E Nichols; H K Lamb; S Cocklin; A Dodds; A R Hawkins
Journal:  EMBO J       Date:  2001-12-03       Impact factor: 11.598

3.  Multiple sequence alignment with the Clustal series of programs.

Authors:  Ramu Chenna; Hideaki Sugawara; Tadashi Koike; Rodrigo Lopez; Toby J Gibson; Desmond G Higgins; Julie D Thompson
Journal:  Nucleic Acids Res       Date:  2003-07-01       Impact factor: 16.971

4.  Prediction of coenzyme specificity in dehydrogenases/reductases. A hidden Markov model-based method and its application on complete genomes.

Authors:  Yvonne Kallberg; Bengt Persson
Journal:  FEBS J       Date:  2006-03       Impact factor: 5.542

5.  Structural analyses of mutant and wild-type alcohol dehydrogenases from drosophila melanogaster.

Authors:  M F Schwartz; H Jörnvall
Journal:  Eur J Biochem       Date:  1976-09

6.  Characteristics of short-chain alcohol dehydrogenases and related enzymes.

Authors:  B Persson; M Krook; H Jörnvall
Journal:  Eur J Biochem       Date:  1991-09-01

7.  NCBI reference sequences (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins.

Authors:  Kim D Pruitt; Tatiana Tatusova; Donna R Maglott
Journal:  Nucleic Acids Res       Date:  2006-11-27       Impact factor: 16.971

8.  The Universal Protein Resource (UniProt).

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Journal:  Nucleic Acids Res       Date:  2005-01-01       Impact factor: 16.971

Review 9.  Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes.

Authors:  K L Kavanagh; H Jörnvall; B Persson; U Oppermann
Journal:  Cell Mol Life Sci       Date:  2008-12       Impact factor: 9.261

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Journal:  PLoS One       Date:  2008-01-23       Impact factor: 3.240

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Journal:  J Bacteriol       Date:  2017-04-25       Impact factor: 3.490

2.  Structural insight into substrate differentiation of the sugar-metabolizing enzyme galactitol dehydrogenase from Rhodobacter sphaeroides D.

Authors:  Yvonne Carius; Henning Christian; Annette Faust; Ulrich Zander; Björn U Klink; Petra Kornberger; Gert-Wieland Kohring; Friedrich Giffhorn; Axel J Scheidig
Journal:  J Biol Chem       Date:  2010-04-21       Impact factor: 5.157

3.  Crystallization and preliminary X-ray analysis of SDR-type pyridoxal dehydrogenase from Mesorhizobium loti.

Authors:  Huy Nhat Chu; Jun Kobayashi; Yu Yoshikane; Bunzo Mikami; Toshiharu Yagi
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-05-29

4.  Crystallization and preliminary X-ray crystallographic analysis of the short-chain dehydrogenase/reductase-type DDB_G0291732 protein from Dictyostelium discoideum.

Authors:  Min Kyu Kim; Hyung Soon Yim; Sa Ouk Kang
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-12-23

Review 5.  Challenges in the annotation of pseudoenzymes in databases: the UniProtKB approach.

Authors:  Rossana Zaru; Michele Magrane; Sandra Orchard
Journal:  FEBS J       Date:  2019-11-03       Impact factor: 5.542

Review 6.  High-throughput structural biology of metabolic enzymes and its impact on human diseases.

Authors:  Wyatt W Yue; Udo Oppermann
Journal:  J Inherit Metab Dis       Date:  2011-02-22       Impact factor: 4.982

7.  Human ortholog of a plant salicylic acid receptor found in SK-N-SH cell line.

Authors:  Hanna Skubatz; William N Howald
Journal:  Protein J       Date:  2013-12       Impact factor: 2.371

8.  Homozygous and compound-heterozygous mutations in TGDS cause Catel-Manzke syndrome.

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Journal:  Am J Hum Genet       Date:  2014-12-04       Impact factor: 11.025

9.  Structural basis for substrate specificity in human monomeric carbonyl reductases.

Authors:  Ewa S Pilka; Frank H Niesen; Wen Hwa Lee; Yasser El-Hawari; James E Dunford; Grazyna Kochan; Vladimir Wsol; Hans-Joerg Martin; Edmund Maser; Udo Oppermann
Journal:  PLoS One       Date:  2009-10-20       Impact factor: 3.240

10.  Species used for drug testing reveal different inhibition susceptibility for 17beta-hydroxysteroid dehydrogenase type 1.

Authors:  Gabriele Möller; Bettina Husen; Dorota Kowalik; Leena Hirvelä; Dariusz Plewczynski; Leszek Rychlewski; Josef Messinger; Hubert Thole; Jerzy Adamski
Journal:  PLoS One       Date:  2010-06-08       Impact factor: 3.240

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