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Enzymatic interconversion of active and inactive glucocorticoid hormone is important, and is carried out physiologically by 11beta-hydroxysteroid dehydrogenase (11beta-HSD) isoforms, explaining their role in cellular and toxicological processes. Two forms of the enzyme, 11beta-HSD-1 and 11beta-HSD-2, belonging to the protein superfamily of short-chain dehydrogenases/reductases, have been structurally and functionally characterised. Although displaying dehydrogenase and reductase activities in vitro, the dominant in vivo function of the type-1 enzyme might be to work as a reductase, thus generating active cortisol from inactive cortisone precursors. On the other hand, for adrenal glucocorticoids the type-2 enzyme seems to be exclusively a dehydrogenase and, by inactivating glucocorticoids, confers specificity to peripheral mineralocorticoid receptors.

Original publication

DOI

10.1111/j.1432-1033.1997.t01-1-00355.x

Type

Journal article

Journal

European journal of biochemistry

Publication Date

10/1997

Volume

249

Pages

355 - 360

Addresses

Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. udo.oppermann@mbb.ki.se

Keywords

Animals, Mammals, Humans, Isoenzymes, Hydroxysteroid Dehydrogenases, 11-beta-Hydroxysteroid Dehydrogenases, Sequence Alignment, Amino Acid Sequence, Protein Conformation, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Substrate Specificity, Models, Structural, Molecular Sequence Data