短链脱氢酶

現有可用的蛋白結構：
Pfam	結構（旧版） / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum（英语：PDBsum）	結構概要

short chain dehydrogenase
short chain dehydrogenase
鑑定
標誌	adh_short
Pfam	PF00106（旧版）
InterPro（英语：InterPro）	IPR002198
PROSITE（英语：PROSITE）	PDOC00060
SCOP（英语：Structural Classification of Proteins）	1hdc / SUPFAM
OPM（英语：Orientations of Proteins in Membranes database）家族	119
OPM（英语：Orientations of Proteins in Membranes database）蛋白	1xu7
CDD（英语：Conserved Domain Database）	cd02266
膜蛋白數據庫（英语：Membranome）	246
Pfam
現有可用的蛋白結構：
Pfam	結構（旧版） / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum（英语：PDBsum）	結構概要

短链脱氢酶（英語：Short-chain dehydrogenase，或称为短链脱氢/还原酶家族，英語：short-chain dehydrogenases/reductases family，缩写SDR）^[2]是一个非常大的蛋白质家族，属于 NAD- 或 NADP-依赖的氧化還原酶，第一个被鉴定的家族成员是黑腹果蝇的醇脱氢酶，因此命名为“昆虫型”（'insect-type'）或“短链”（'short-chain'）醇脱氢酶^[3]^[4]^[5]。大部分酶家族成员有250到300个氨基酸残基，且包含至少两个结构域^[6]其中一个用于结合辅酶，大部分是NAD，少部分是NADP，另一个用于结合底物及催化。

人类基因组中的成员

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;

参考文献

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

[pmid7866748-1] Ghosh D, Erman M, Wawrzak Z, Duax WL, Pangborn W. Mechanism of inhibition of 3 alpha, 20 beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor. Structure. October 1994, 2 (10): 973–80. PMID 7866748. doi:10.1016/S0969-2126(94)00099-9.

[PUB00000419-2] Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D, Jornvall H. Short-chain dehydrogenases/reductases (SDR). Biochemistry. 1995, 34 (18): 6003–6013. PMID 7742302. doi:10.1021/bi00039a038.

[PUB00001371-3] Villarroya A, Juan E, Egestad B, Jornvall H. The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. Eur. J. Biochem. 1989, 180 (1): 191–197. PMID 2707261. doi:10.1111/j.1432-1033.1989.tb14632.x.

[PUB00001399-4] Persson B, Krook M, Jornvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 1991, 200 (2): 537–543. PMID 1889416. doi:10.1111/j.1432-1033.1991.tb16215.x.

[PUB00001408-5] Harayama S, Bairoch A, Hartnett C, Rekik M, Ornston LN, Neidle E. 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. 1992, 204 (1): 113–120. PMID 1740120. doi:10.1111/j.1432-1033.1992.tb16612.x.

[PUB00004592-6] Benyajati C, Place AR, Powers DA, Sofer W. Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein. Proc. Natl. Acad. Sci. U.S.A. 1981, 78 (5): 2717–2721. PMC 319428  . PMID 6789320. doi:10.1073/pnas.78.5.2717.

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