SORD

SORD
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1PL8, 1PL6, 1PL7
Identifiers
Aliases	SORD, HEL-S-95n, SORD1, sorbitol dehydrogenase, XDH, RDH, SDH
External IDs	OMIM: 182500 MGI: 98266 HomoloGene: 56080 GeneCards: SORD
Gene location (Human)
Chr.	Chromosome 15 (human)[1]
End	45,077,185 bp[1]
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)[2]
End	122,265,340 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• NAD binding; • zinc ion binding; • metal ion binding; • L-iditol 2-dehydrogenase activity; • oxidoreductase activity; • D-xylulose reductase activity; • carbohydrate binding; • identical protein binding; • (R,R)-butanediol dehydrogenase activity; • ribitol 2-dehydrogenase activity;
Cellular component	• cytosol; • cell projection; • membrane; • mitochondrial membranes; • cilium; • mitochondrion; • motile cilium; • extracellular exosome; • extracellular;
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
Orthologs
	6652
	20322
	ENSG00000140263
	ENSMUSG00000027227
	Q00796
	Q64442
	NM_003104
	NM_146126
	NP_003095
	NP_666238
	Wikidata
View/Edit Human	View/Edit Mouse

Sorbitol dehydrogenase is an enzyme that in humans is encoded by the SORD gene.[5][6]

References

GRCh38: Ensembl release 89: ENSG00000140263 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000027227 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.

External links

Overview of all the structural information available in the PDB for UniProt: Q00796 (Sorbitol dehydrogenase) at the PDBe-KB.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000140263 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000027227 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7782086-5] 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-6] "Entrez Gene: SORD sorbitol dehydrogenase".

SORD

References

Further reading

External links