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

RefSeq (mRNA)

RefSeq (protein)

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.^[1]^[2]

References

^ 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.
^ "Entrez Gene: SORD sorbitol dehydrogenase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6652.

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.

PDB gallery

1pl6: Human SDH/NADH/inhibitor complex

1pl7: Human Sorbitol Dehydrogenase (apo)

1pl8: human SDH/NAD+ complex

SORD

References

Further reading