SORD

Not to be confused with Sword.

For the computer company, see Sord Computer Corporation.

Sorbitol dehydrogenase
PDB rendering based on 1pl6.
Available structures PDB 1PL6, 1PL7, 1PL8
Identifiers
Symbols	SORD; SORD1
External IDs	OMIM: 182500 MGI: 98266 HomoloGene: 56080 GeneCards: SORD Gene
EC number	1.1.1.14
Gene Ontology Molecular function • L-iditol 2-dehydrogenase activity • L-iditol 2-dehydrogenase activity • binding • sugar binding • zinc ion binding • zinc ion binding • oxidoreductase activity • metal ion binding • NAD binding Cellular component • extracellular space • membrane fraction • soluble fraction • soluble fraction • mitochondrion • cilium • membrane • flagellum • mitochondrial membrane Biological process • glucose metabolic process • sorbitol catabolic process • sperm motility • fructose biosynthetic process • L-xylitol catabolic process • L-xylitol metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6652	20322
Ensembl	ENSG00000140263	ENSMUSG00000027227
UniProt	Q00796	Q569V5
RefSeq (mRNA)	NM_003104.5	NM_146126.4
RefSeq (protein)	XP_001132175	NP_666238.1
Location (UCSC)	Chr 15: 45.32 – 45.37 Mb	Chr 2: 122.06 – 122.09 Mb
PubMed search	[1]	[2]

Sorbitol dehydrogenase is an enzyme that in humans is encoded by the SORD gene.

Further reading

• El-Kabbani O, Darmanin C, Chung RP (2004). "Sorbitol dehydrogenase: structure, function and ligand design.". Curr. Med. Chem. 11 (4): 465–76. doi:10.2174/0929867043455927. PMID 14965227. 
• Karlsson C, Maret W, Auld DS, et al. (1990). "Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme.". Eur. J. Biochem. 186 (3): 543–50. doi:10.1111/j.1432-1033.1989.tb15240.x. PMID 2691249. 
• Samanta BK, Chandra NC, Ghosh S, Mukherjee KL (1985). "Aldose metabolism in developing human fetal brain and liver.". Experientia 40 (12): 1420–2. doi:10.1007/BF01951922. PMID 6439573. 
• Lee FK, Lee AY, Lin CX, et al. (1995). "Cloning, sequencing, and determination of the sites of expression of mouse sorbitol dehydrogenase cDNA.". Eur. J. Biochem. 230 (3): 1059–65. doi:10.1111/j.1432-1033.1995.tb20656.x. PMID 7601136. 
• Lee FK, Cheung MC, Chung S (1994). "The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization.". Genomics 21 (2): 354–8. doi:10.1006/geno.1994.1276. PMID 8088829. 
• Alvarez A, Martínez A, Ibarra B, et al. (1993). "Membrane-bound sorbitol dehydrogenase in human red blood cells. Studies in normal subjects and in enzyme-deficient subjects with congenital cataracts.". J. Inherit. Metab. Dis. 16 (1): 67–72. doi:10.1007/BF00711317. PMID 8487505. 
• Carr IM, Markham AF, Coletta PL (1997). "Identification and characterisation of a sequence related to human sorbitol dehydrogenase.". Eur. J. Biochem. 245 (3): 760–7. doi:10.1111/j.1432-1033.1997.00760.x. PMID 9183016. 
• Carr IM, Whitehouse A, Coletta PL, Markham AF (1999). "Structural and evolutionary characterization of the human sorbitol dehydrogenase gene duplication.". Mamm. Genome 9 (12): 1042–8. doi:10.1007/s003359900922. PMID 9880675. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Darmanin C, Iwata T, Carper DA, et al. (2003). "Expression, purification and preliminary crystallographic analysis of human sorbitol dehydrogenase.". Acta Crystallogr. D Biol. Crystallogr. 59 (Pt 3): 558–60. doi:10.1107/S0907444903000441. PMID 12595725. 
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. 
• Pauly TA, Ekstrom JL, Beebe DA, et al. (2004). "X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase.". Structure 11 (9): 1071–85. doi:10.1016/S0969-2126(03)00167-9. PMID 12962626. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Pope SN, Lee IR (2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin.". J. Steroid Biochem. Mol. Biol. 94 (1–3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Klimacek M, Hellmer H, Nidetzky B (2007). "Catalytic mechanism of Zn2+-dependent polyol dehydrogenases: kinetic comparison of sheep liver sorbitol dehydrogenase with wild-type and Glu154-->Cys forms of yeast xylitol dehydrogenase". Biochem. J. 404 (3): 421–9. doi:10.1042/BJ20061384. PMC 1896283. PMID 17343568. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1896283.