HSD17B14
HSD17B14 (hydroxysteroid 17-beta dehydrogenase 14) is a cytoplasmic member of the short-chain dehydrogenase/reductase superfamily. UniProt names it L-fucose dehydrogenase, and it is also known as retSDR3, SDR47C1 and DHRS10. Browse Assay Genie's current range of HSD17B14 research reagents below, or read on for the biology behind the target.
HSD17B14 catalyses the NAD(+)-dependent oxidation of L-fucose, yielding L-fucono-1,5-lactone, which rapidly converts spontaneously to L-fucone-1,4-lactone. It can also act on D-arabinose and L-galactose, but with lower catalytic efficiency. The enzyme does not use NADPH. On this basis it may be the initial enzyme of the L-fucose degradation pathway in mammals.
The HSD17B14 gene encodes a protein that belongs to the short-chain dehydrogenases/reductases (SDR) family, and HGNC places it in the short chain dehydrogenase/reductase superfamily. The protein is found in the cytoplasm. Researchers studying HSD17B14 at the protein level will often work with the enzyme in the context of other SDR family members and related hydroxysteroid dehydrogenases.
The name reflects the wider group of 17-beta-hydroxysteroid dehydrogenases. According to the NCBI Gene summary, these enzymes, including HSD17B14, are primarily involved in metabolism of steroids at the C17 position and also of other substrates, such as fatty acids, prostaglandins and xenobiotics. Earlier names for the gene include dehydrogenase/reductase (SDR family) member 10 and hydroxysteroid (17-beta) dehydrogenase 14, with the symbols DHRS10, retSDR3 and SDR47C1 also in use. Orthologues are annotated in mouse and rat as Hsd17b14.
HSD17B14 may be the initial enzyme of the L-fucose degradation pathway in mammals, making it a focus for studies of fucose catabolism.
The enzyme acts on L-fucose, and with lower efficiency on D-arabinose and L-galactose, which makes it useful for studying SDR substrate preference.
As a 17-beta-hydroxysteroid dehydrogenase family member, it relates to metabolism of steroids, fatty acids, prostaglandins and xenobiotics.
HSD17B14 uses NAD(+) and does not use NADPH, providing a defined example for work on cofactor selectivity in SDR enzymes.
HSD17B14 catalyses the NAD(+)-dependent oxidation of L-fucose to L-fucono-1,5-lactone, which converts spontaneously to L-fucone-1,4-lactone. It can also act on D-arabinose and L-galactose with lower efficiency, does not use NADPH, and may start the L-fucose degradation pathway in mammals.
HSD17B14 is also called retSDR3, SDR47C1 and DHRS10. Previous names are dehydrogenase/reductase (SDR family) member 10 and hydroxysteroid (17-beta) dehydrogenase 14. UniProt lists the protein as L-fucose dehydrogenase, with the EC number 1.1.1.122.
Yes. Orthologues of the HSD17B14 gene are annotated in both mouse and rat, where the symbol is Hsd17b14. This allows rodent models to be used for work on the enzyme; check the datasheet of any product for its validated reactivity.
Other hydroxysteroid dehydrogenases and short-chain dehydrogenase/reductase family enzymes involved in steroid and small-molecule metabolism.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9BPX1; product specifications from Assay Genie datasheets.