| 词条 | Short-chain dehydrogenase |
| 释义 |
| Symbol = adh_short | Name = short chain dehydrogenase | image = PDB 1hdc EBI.jpg | width = | caption = [1] | Pfam= PF00106 | InterPro= IPR002198 | SMART= | PROSITE = PDOC00060 | SCOP = 1hdc | TCDB = | OPM family= 119 | OPM protein= 1xu7 | CDD = cd02266 | PDB= | Membranome superfamily = 246 }}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] Subfamilies
Human proteins containing this domain17BHSDI; 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; References1. ^{{cite journal |vauthors=Ghosh D, Erman M, Wawrzak Z, Duax WL, Pangborn W |title=Mechanism of inhibition of 3 alpha, 20 beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor |journal=Structure |volume=2 |issue=10 |pages=973–80 |date=October 1994 |pmid=7866748 |doi= 10.1016/S0969-2126(94)00099-9|url=}} 2. ^{{cite journal |vauthors=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}} 3. ^{{cite journal |vauthors=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}} 4. ^{{cite journal |vauthors=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}} 5. ^{{cite journal |vauthors=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}} 6. ^1 {{cite journal |vauthors=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 |pmc=319428}} 2 : Protein domains|Single-pass transmembrane proteins |
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