Journal
JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY
Volume 117, Issue 4-5, Pages 117-124Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jsbmb.2009.08.001
Keywords
Short-chain dehydrogenase/reductase (SDR); SDR-orphan (SDR-O); Retinal; Hydroxysteroid dehydrogenase-like 2 (HSDL2); Sterol carrier protein 2 (SCP2)
Funding
- Bayerische Forschungsstiftung [606/04]
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The protein superfamily of short-chain dehydrogenases/reductases (SDRs) today comprises over 20,000 members found in pro- and eukaryotes. Despite low amino acid sequence identity (only 15-30%), they share several similar characteristics in conformational structures, the N-terminal cofactor (NAD(P)/NAD(P)H) binding region being the most conserved. The enzymes catalyze oxido-reductive reactions and have a broad spectrum of substrates. Not all recently identified SDRs have been analyzed in detail yet, and we therefore characterized two rudimentarily annotated human SDR candidates: an orphan SDR (SDR-O) and hydroxysteroid dehydrogenase like 2 (HSDL2). We analyzed the amino acid sequence for cofactor preference, performed subcellular localization studies, and a screening for substrates of the enzymes, including steroid hormones and retinoids. None of both tested proteins showed a significant conversion of steroid hormones. However, the peroxisomal localization of human HSDL2 may suggest an involvement in fatty acid metabolism. For SDR-O a weak conversion of retinal into retinol was detectable in the presence of the cofactor NADH. (C) 2009 Elsevier Ltd. All rights reserved.
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