Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Most mammalian hydroxysteroid dehydrogenases known thus far belong to the protein superfamilies of short-chain dehydrogenases/reductases (SDR) and aldo-keto reductases (AKR). Whereas members of the AKR family are soluble, cytoplasmic enzymes, SDR-type hydroxysteroid dehydrogenases are also located to other subcellular compartments, i.e. endoplasmic reticulum, mitochondria or peroxisomes. Differential localization might play an important role in influencing the reaction direction of hydroxy dehydrogenase/oxo reductase pathways by determining the available nucleotide cofactor pool. Targeting signals for different subcellular organelles in human hydroxysteroid dehydrogenases have been identified, however, in several enzymes localization signals remain to be determined.

Original publication

DOI

10.1016/s0303-7207(00)00419-6

Type

Journal article

Journal

Mol Cell Endocrinol

Publication Date

22/01/2001

Volume

171

Pages

99 - 101

Keywords

11-beta-Hydroxysteroid Dehydrogenases, Amino Acid Sequence, Animals, COS Cells, Cell Membrane, Endoplasmic Reticulum, Green Fluorescent Proteins, Humans, Hydroxysteroid Dehydrogenases, Isoenzymes, Luminescent Proteins, Microscopy, Fluorescence, Mitochondria, Molecular Sequence Data, Peptide Fragments, Peroxisomes, Recombinant Fusion Proteins, Sequence Alignment, Subcellular Fractions, Transfection