PuSH - Publikationsserver des Helmholtz Zentrums München

Kowalik, D. ; Haller, F. ; Adamski, J. ; Möller, G.

In search for function of two human orphan SDR enzymes: Hydroxysteroid dehydrogenase like 2 (HSDL2) and short-chain degydrogenase/reductase-orphan (SDR-O).

J. Steroid Biochem. Mol. Biol. 117, 117-124 (2009)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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.
Altmetric
Weitere Metriken?
[➜Einloggen]
Zusatzinfos bearbeiten [➜Einloggen]
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Base Sequence; Cell Line; Cloning, Molecular; DNA Primers; Humans; Hydroxysteroid; ehydrogenases/metabolism*; Oxidoreductases/metabolism*; Recombinant Proteins/metabolism; Subcellular Fractions/enzymology; Substrate Specificity
ISSN (print) / ISBN 0960-0760
e-ISSN 0960-0760
Zeitschrift Journal of Steroid Biochemistry and Molecular Biology, The
Quellenangaben Band: 117, Heft: 4-5, Seiten: 117-124 Artikelnummer: , Supplement: ,
Verlag Elsevier
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Molekulare Endokrinologie und Metabolismus (MEM)