Short-chain dehydrogenase

The short-chain dehydrogenases/reductases family (SDR)[2] 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 called[3][4][5] 'insect-type', or 'short-chain' alcohol dehydrogenases. Most members of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domains,[6] 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.[6]

short chain dehydrogenase
Identifiers
Symboladh_short
PfamPF00106
InterProIPR002198
PROSITEPDOC00060
SCOPe1hdc / SUPFAM
OPM superfamily119
OPM protein1xu7
CDDcd02266
Membranome246

Subfamilies

Human proteins containing this domain

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;

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References
  1. Ghosh D, Erman M, Wawrzak Z, Duax WL, Pangborn W (October 1994). "Mechanism of inhibition of 3 alpha, 20 beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor". Structure. 2 (10): 973–80. doi:10.1016/S0969-2126(94)00099-9. PMID 7866748.
  2. Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D, Jornvall H (1995). "Short-chain dehydrogenases/reductases (SDR)". Biochemistry. 34 (18): 6003–6013. doi:10.1021/bi00039a038. PMID 7742302.
  3. Villarroya A, Juan E, Egestad B, Jornvall H (1989). "The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc". Eur. J. Biochem. 180 (1): 191–197. doi:10.1111/j.1432-1033.1989.tb14632.x. PMID 2707261.
  4. Persson B, Krook M, Jornvall H (1991). "Characteristics of short-chain alcohol dehydrogenases and related enzymes". Eur. J. Biochem. 200 (2): 537–543. doi:10.1111/j.1432-1033.1991.tb16215.x. PMID 1889416.
  5. Harayama S, Bairoch A, Hartnett C, Rekik M, Ornston LN, Neidle E (1992). "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". Eur. J. Biochem. 204 (1): 113–120. doi:10.1111/j.1432-1033.1992.tb16612.x. PMID 1740120.
  6. Benyajati C, Place AR, Powers DA, Sofer W (1981). "Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein". Proc. Natl. Acad. Sci. U.S.A. 78 (5): 2717–2721. doi:10.1073/pnas.78.5.2717. PMC 319428. PMID 6789320.
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