SORD

Sorbitol dehydrogenase
PDB rendering based on 1pl6.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1PL6​, 1PL7​, 1PL8​
Identifiers
Symbols	SORD ; HEL-S-95n; SORD1
External IDs	OMIM: 182500 MGI: 98266 HomoloGene: 56080 ChEMBL: 2275 GeneCards: SORD Gene
EC number	1.1.1.14
Gene ontology Molecular function • L-iditol 2-dehydrogenase activity • zinc ion binding • carbohydrate binding • identical protein binding • NAD binding Cellular component • extracellular space • cytosol • membrane • motile cilium • mitochondrial membrane • extracellular exosome Biological process • carbohydrate metabolic process • fructose metabolic process • glucose metabolic process • sorbitol catabolic process • response to osmotic stress • response to hormone • sperm motility • response to nutrient levels • response to drug • small molecule metabolic process • fructose biosynthetic process • response to cadmium ion • response to copper ion • L-xylitol catabolic process • L-xylitol metabolic process • oxidation-reduction process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6652	20322
Ensembl	ENSG00000140263	ENSMUSG00000027227
UniProt	Q00796	Q64442
RefSeq (mRNA)	NM_003104	NM_146126
RefSeq (protein)	NP_003095	NP_666238
Location (UCSC)	Chr 15: 45.02 – 45.08 Mb	Chr 2: 122.23 – 122.27 Mb
PubMed search

Sorbitol dehydrogenase is an enzyme that in humans is encoded by the SORD gene.^[1][2]

References

1. Iwata T, Popescu NC, Zimonjic DB, Karlsson C, Hoog JO, Vaca G, Rodriguez IR, Carper D (Jul 1995). "Structural organization of the human sorbitol dehydrogenase gene (SORD)". Genomics 26 (1): 55–62. doi:10.1016/0888-7543(95)80082-W. PMID 7782086.
2. "Entrez Gene: SORD sorbitol dehydrogenase".

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.
• 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.
• 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.