SORD

Not to be confused with Sword.

For the computer company, see Sord Computer Corporation.

SORD

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1PL8, 1PL6, 1PL7

Identifiers

Aliases

SORD, HEL-S-95n, SORD1, sorbitol dehydrogenase

External IDs

MGI: 98266 HomoloGene: 56080 GeneCards: SORD

Gene ontology
Molecular function	• NAD binding • zinc ion binding • metal ion binding • identical protein binding • L-iditol 2-dehydrogenase activity • oxidoreductase activity • D-xylulose reductase activity • carbohydrate binding
Cellular component	• cytosol • cell projection • membrane • mitochondrial membrane • cilium • extracellular fluid • mitochondrion • motile cilium • extracellular exosome
Biological process	• flagellated sperm motility • response to cadmium ion • response to copper ion • sorbitol catabolic process • fructose biosynthetic process • glucuronate catabolic process to xylulose 5-phosphate • response to osmotic stress • L-xylitol metabolic process • response to nutrient levels • glucose metabolic process • L-xylitol catabolic process • response to hormone • sorbitol metabolic process • oxidation-reduction process • response to drug
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_003095.2


NP_666238.1

Location (UCSC)

Chr 15: 45.02 – 45.08 Mb

Chr 2: 122.23 – 122.27 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Sorbitol dehydrogenase is an enzyme that in humans is encoded by the SORD gene.^[3]^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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".

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. 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.

PDB gallery

1pl6: Human SDH/NADH/inhibitor complex

1pl7: Human Sorbitol Dehydrogenase (apo)

1pl8: human SDH/NAD+ complex

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SORD

References

Further reading