SORD

"SORD (gene)" redirects here. For other uses, see 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, SORDD
External IDs	OMIM: 182500; MGI: 98266; HomoloGene: 56080; GeneCards: SORD; OMA:SORD - orthologs
Gene location (Human) Chr. Chromosome 15 (human) [1] Band 15q21.1 Start 45,023,147 bp [1] End 45,077,185 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2 E5|2 60.59 cM Start 122,065,230 bp [2] End 122,095,821 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of thyroid gland left lobe of thyroid gland right lobe of liver olfactory zone of nasal mucosa prostate right adrenal cortex left adrenal gland left adrenal cortex islet of Langerhans ventricular zone Top expressed in seminiferous tubule spermatid right kidney spermatocyte left lobe of liver human kidney seminal vesicula morula blastocyst myocardium of ventricle More reference expression data BioGPS 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 space 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 Sources:Amigo / QuickGO
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: 122.07 – 122.1 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

References

1. GRCh38: Ensembl release 89: ENSG00000140263 – Ensembl, May 2017
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.
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.
6. "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. S2CID   2545958.
• 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 (inactive 20 October 2025). 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. S2CID   6783099.
• 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. S2CID   21773145.
• 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. Bibcode:2002PNAS...9916899M. 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. S2CID   23783563.
• 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. S2CID   9746088.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• 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 .