Literature DB >> 19061874

The human short-chain dehydrogenase/reductase (SDR) superfamily: a bioinformatics summary.

James E Bray1, Brian D Marsden, Udo Oppermann.   

Abstract

The short-chain dehydrogenase/reductase (SDR) superfamily represents one of the largest protein superfamilies known to date. Enzymes of this family usually catalyse NAD(P)(H) dependent reactions with a substrate spectrum ranging from polyols, retinoids, steroids and fatty acid derivatives to xenobiotics. We have currently identified 73 SDR superfamily members within the human genome. A status report of the human SDR superfamily is provided in terms of 3D structure determination, co-factor preferences, subcellular localisation and functional annotation. A simple scoring system for measuring structural and functional information (SFS score) has also been introduced to monitor the status of 5 key metrics. Currently there are 17 SDR members with an SFS score of zero indicating that almost a quarter of the human SDR superfamily lacks substantial functional annotation.

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Year:  2008        PMID: 19061874     DOI: 10.1016/j.cbi.2008.10.058

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


  31 in total

Review 1.  Structural insights into the functional versatility of WW domain-containing oxidoreductase tumor suppressor.

Authors:  Amjad Farooq
Journal:  Exp Biol Med (Maywood)       Date:  2015-02-07

2.  Human dehydrogenase/reductase (SDR family) member 8 (DHRS8): a description and evaluation of its biochemical properties.

Authors:  Tereza Lundová; Hana Štambergová; Lucie Zemanová; Markéta Svobodová; Jana Havránková; Miroslav Šafr; Vladimír Wsól
Journal:  Mol Cell Biochem       Date:  2015-10-16       Impact factor: 3.396

3.  In silico structure-function analysis of pathological variation in the HSD11B2 gene sequence.

Authors:  Jonathan R Manning; Matthew A Bailey; Dinesh C Soares; Donald R Dunbar; John J Mullins
Journal:  Physiol Genomics       Date:  2010-06-22       Impact factor: 3.107

4.  Beta hydroxylation of glycolipids from Ustilago maydis and Pseudozyma flocculosa by an NADPH-dependent β-hydroxylase.

Authors:  Beate Teichmann; François Lefebvre; Caroline Labbé; Michael Bölker; Uwe Linne; Richard R Bélanger
Journal:  Appl Environ Microbiol       Date:  2011-09-16       Impact factor: 4.792

5.  Molecular modeling of the reaction pathway and hydride transfer reactions of HMG-CoA reductase.

Authors:  Brandon E Haines; C Nicklaus Steussy; Cynthia V Stauffacher; Olaf Wiest
Journal:  Biochemistry       Date:  2012-09-25       Impact factor: 3.162

6.  15-Oxoeicosatetraenoic acid is a 15-hydroxyprostaglandin dehydrogenase-derived electrophilic mediator of inflammatory signaling pathways.

Authors:  Nathaniel W Snyder; Franca Golin-Bisello; Yang Gao; Ian A Blair; Bruce A Freeman; Stacy Gelhaus Wendell
Journal:  Chem Biol Interact       Date:  2014-11-04       Impact factor: 5.192

Review 7.  Role of WW domain proteins WWOX in development, prognosis, and treatment response of glioma.

Authors:  Shin-Yi Liu; Ming-Fu Chiang; Yu-Jen Chen
Journal:  Exp Biol Med (Maywood)       Date:  2014-11-27

8.  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

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

Review 10.  AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders.

Authors:  Trevor M Penning
Journal:  Mol Cell Endocrinol       Date:  2018-09-19       Impact factor: 4.102

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