Short-chain dehydrogenase

The short-chain dehydrogenases/reductases family (SDR)cite journal |author=Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D, Jornvall H |title=Short-chain dehydrogenases/reductases (SDR) |journal=Biochemistry |volume=34 |issue=18 |pages=6003–6013 |year=1995 |pmid=7742302 |doi=10.1021/bi00039a038] is a very large family of enzymes, most of which are known to be NAD- or NADP-dependent oxidoreductases. As the first member of this family to be characterised was Drosophila alcohol dehydrogenase, this family used to be calledcite journal |author=Villarroya A, Juan E, Egestad B, Jornvall H |title=The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc |journal=Eur. J. Biochem. |volume=180 |issue=1 |pages=191–197 |year=1989 |pmid=2707261 |doi=10.1111/j.1432-1033.1989.tb14632.x] cite journal |author=Persson B, Krook M, Jornvall H |title=Characteristics of short-chain alcohol dehydrogenases and related enzymes |journal=Eur. J. Biochem. |volume=200 |issue=2 |pages=537–543 |year=1991 |pmid=1889416 |doi=10.1111/j.1432-1033.1991.tb16215.x] cite journal |author=Harayama S, Bairoch A, Hartnett C, Rekik M, Ornston LN, Neidle E |title=cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily |journal=Eur. J. Biochem. |volume=204 |issue=1 |pages=113–120 |year=1992 |pmid=1740120 |doi=10.1111/j.1432-1033.1992.tb16612.x] 'insect-type', or 'short-chain' alcohol dehydrogenases. Most member of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domainscite journal |author=Benyajati C, Place AR, Powers DA, Sofer W |title=Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=78 |issue=5 |pages=2717–2721 |year=1981 |pmid=6789320 |doi=10.1073/pnas.78.5.2717] , the first binding the coenzyme, often NAD, and the second binding the substrate. This latter domain determines the substrate specificity and contains amino acids involved in catalysis. Little sequence similarity has been found in the coenzyme binding domain although there is a large degree of structural similarity, and it has therefore been suggested that the structure of dehydrogenases has arisen through gene fusion of a common ancestral coenzyme nucleotide sequence with various substrate specific domains.

ubfamilies

*Glucose/ribitol dehydrogenase InterPro|IPR002347
*Insect alcohol dehydrogenase family InterPro|IPR002424
*2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase InterPro|IPR003560

Human proteins containing this domain

17BHSDI; BDH1; BDH2; CBR1; CBR3; CBR4; DCXR; DECR1;
DECR2; DHRS1; DHRS10; DHRS13; DHRS2; DHRS3; DHRS4; DHRS4L2;
DHRS7; DHRS7B; DHRS8; DHRS9; DHRSX; FASN; FVT1; HADH2;
HPGD; HSD11B1; HSD11B2; HSD17B1; HSD17B10; HSD17B12; HSD17B13; HSD17B2;
HSD17B3; HSD17B4; HSD17B6; HSD17B7; HSD17B7P2; HSD17B8; HSDL1; HSDL2;
PECR; QDPR; RDH10; RDH11; RDH12; RDH13; RDH14; RDH16;
RDH5; RDH8; RDHE2; RDHS; SCDR10; SPR; WWOX;

References

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