[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/udp-glucose-6-dehydrogenase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/udp-glucose-6-dehydrogenase-wikipedia\/","headline":"UDP-glucose 6-dehydrogenase – Wikipedia","name":"UDP-glucose 6-dehydrogenase – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Mammalian protein found in Homo sapiens UGDH Available structures PDB Ortholog search: PDBe","datePublished":"2017-07-09","dateModified":"2017-07-09","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/6\/63\/Protein_UGDH_PDB_2Q3E.png\/250px-Protein_UGDH_PDB_2Q3E.png","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/6\/63\/Protein_UGDH_PDB_2Q3E.png\/250px-Protein_UGDH_PDB_2Q3E.png","height":"208","width":"250"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/udp-glucose-6-dehydrogenase-wikipedia\/","wordCount":5834,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Mammalian protein found in Homo sapiensUGDHAvailable structuresPDBOrtholog search: PDBe RCSB List of PDB id codes2Q3E, 2QG4, 3ITK, 3KHU, 3PRJ, 3PTZ, 3TDK, 3TF5, 4EDF, 4QEJ, 4RJT       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4IdentifiersAliasesUGDH, GDH, UDP-GlcDH, UDPGDH, UGD, UDP-glucose 6-dehydrogenase, EIEE84, DEE84External IDsOMIM: 603370 MGI: 1306785 HomoloGene: 2520 GeneCards: UGDH WikidataUDP-glucose 6-dehydrogenase is a cytosolic enzyme that in humans is encoded by the UGDH gene.[5][6][7]The protein encoded by this gene converts UDP-glucose to UDP-glucuronate and thereby participates in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated compounds are common components of the extracellular matrix and likely play roles in signal transduction, cell migration, and cancer growth and metastasis. The expression of this gene is up-regulated by transforming growth factor beta and down-regulated by hypoxia.[7]This enzyme participates in 4 metabolic pathways: pentose and glucuronate interconversions, ascorbate and aldarate metabolism, starch and sucrose metabolism, and nucleotide sugars metabolism.Loss of UGDH has recently been implicated in epileptic encephalopathy in humans[8]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Table of ContentsNomenclature[edit]Biochemistry[edit]References[edit]Further reading[edit]Nomenclature[edit]This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is UDP-glucose:NAD+ 6-oxidoreductase.Other names in common use include:UDP-glucose dehydrogenase,uridine diphosphoglucose dehydrogenase,UDPG dehydrogenase,UDPG:NAD oxidoreductase,UDP-alpha-D-glucose:NAD oxidoreductase,UDP-glucose:NAD+ oxidoreductase,uridine diphosphate glucose dehydrogenase,UDP-D-glucose dehydrogenase, anduridine diphosphate D-glucose dehydrogenase.Biochemistry[edit]In enzymology, a UDP-glucose 6-dehydrogenase (EC 1.1.1.22) is an enzyme that catalyzes the chemical reactionUDP-glucose + 2 NAD+ + H2O \u21cc{displaystyle rightleftharpoons } UDP-glucuronate + 2 NADH + 2 H+The 3 substrates of this enzyme are UDP-glucose, NAD+, and H2O, whereas its 3 products are UDP-glucuronate, NADH, and H+References:[9][10][11][12]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000109814 – Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029201 – 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.^ Spicer AP, Kaback LA, Smith TJ, Seldin MF (Sep 1998). “Molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes”. The Journal of Biological Chemistry. 273 (39): 25117\u201324. doi:10.1074\/jbc.273.39.25117. PMID\u00a09737970.^ Marcu O, Stathakis DG, Marsh JL (Jan 2000). “Assignment of the UGDH locus encoding UDP-glucose dehydrogenase to human chromosome band 4p15.1 by radiation hybrid mapping”. Cytogenetics and Cell Genetics. 86 (3\u20134): 244\u20135. doi:10.1159\/000015350. PMID\u00a010575217. S2CID\u00a025740995.^ a b “Entrez Gene: UGDH UDP-glucose dehydrogenase”.^ Hengel, H., Bosso-Lef\u00e8vre, C., Grady, G. et al. Loss-of-function mutations in UDP-Glucose 6-Dehydrogenase cause recessive developmental epileptic encephalopathy. Nat Commun 11, 595 (2020). https:\/\/doi.org\/10.1038\/s41467-020-14360-7^ Druzhinina TN, Kusov YY, Shibaev VN, Kochetkov NK, Biel\u00fd P, Kuc\u00e1r S, Bauer S (Feb 1975). “Uridine diphosphate 2-deoxyglucose. Chemical synthesis, enzymic oxidation and epimerization”. Biochimica et Biophysica Acta. 381 (2): 301\u20137. doi:10.1016\/0304-4165(75)90236-6. PMID\u00a01091296.^ Kalckar HM, Maxwell ES, Strominger JL (Nov 1956). “Some properties of uridine diphosphoglucose dehydrogenase”. Archives of Biochemistry and Biophysics. 65 (1): 2\u201310. doi:10.1016\/0003-9861(56)90171-0. PMID\u00a013373402.^ Strominger JL, Mapson LW (Aug 1957). “Uridine diphosphoglucose dehydrogenase of pea seedlings”. The Biochemical Journal. 66 (4): 567\u201372. doi:10.1042\/bj0660567. PMC\u00a01200063. PMID\u00a013459898.^ Axelrod J, Kalckar HM, Maxwell ES, Strominger JL (Jan 1957). “Enzymatic formation of uridine diphosphoglucuronic acid”. The Journal of Biological Chemistry. 224 (1): 79\u201390. doi:10.1016\/S0021-9258(18)65012-4. PMID\u00a013398389.Further reading[edit]Peng HL, Lou MD, Chang ML, Chang HY (Oct 1998). “cDNA cloning and expression analysis of the human UDPglucose dehydrogenase”. Proceedings of the National Science Council, Republic of China. Part B, Life Sciences. 22 (4): 166\u201372. PMID\u00a09850599.Bontemps Y, Maquart FX, Wegrowski Y (Sep 2000). “Human UDP-glucose dehydrogenase gene: complete cloning and transcription start mapping”. Biochemical and Biophysical Research Communications. 275 (3): 981\u20135. doi:10.1006\/bbrc.2000.3389. PMID\u00a010973831.Bontemps Y, Vuillermoz B, Antonicelli F, Perreau C, Danan JL, Maquart FX, Wegrowski Y (Jun 2003). “Specific protein-1 is a universal regulator of UDP-glucose dehydrogenase expression: its positive involvement in transforming growth factor-beta signaling and inhibition in hypoxia”. The Journal of Biological Chemistry. 278 (24): 21566\u201375. doi:10.1074\/jbc.M209366200. PMID\u00a012682078.Sommer BJ, Barycki JJ, Simpson MA (May 2004). “Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive oxidations”. The Journal of Biological Chemistry. 279 (22): 23590\u20136. doi:10.1074\/jbc.M401928200. PMID\u00a015044486.Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (Jun 2004). “Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation”. Nature Biotechnology. 22 (6): 707\u201316. doi:10.1038\/nbt971. PMID\u00a015146197. S2CID\u00a027764390.Huh JW, Yoon HY, Lee HJ, Choi WB, Yang SJ, Cho SW (Sep 2004). “Importance of Gly-13 for the coenzyme binding of human UDP-glucose dehydrogenase”. The Journal of Biological Chemistry. 279 (36): 37491\u20138. doi:10.1074\/jbc.M404234200. PMID\u00a015247292.Huh JW, Lee HJ, Choi MM, Yang SJ, Yoon SY, Kim DW, Kim SY, Choi SY, Cho SW (2005). “Identification of a UDP-glucose-binding site of human UDP-glucose dehydrogenase by photoaffinity labeling and cassette mutagenesis”. Bioconjugate Chemistry. 16 (3): 710\u20136. doi:10.1021\/bc0500387. PMID\u00a015898741.Vatsyayan J, Peng HL, Chang HY (Jun 2005). “Analysis of human UDP-glucose dehydrogenase gene promoter: identification of an Sp1 binding site crucial for the expression of the large transcript”. Journal of Biochemistry. 137 (6): 703\u20139. doi:10.1093\/jb\/mvi082. PMID\u00a016002992.Wang L, Zhu YF, Guo XJ, Huo R, Ma X, Lin M, Zhou ZM, Sha JH (Oct 2005). “A two-dimensional electrophoresis reference map of human ovary”. Journal of Molecular Medicine. 83 (10): 812\u201321. doi:10.1007\/s00109-005-0676-y. PMID\u00a016021519. S2CID\u00a06644433.Vatsyayan J, Lin CT, Peng HL, Chang HY (Feb 2006). “Identification of a cis-acting element responsible for negative regulation of the human UDP-glucose dehydrogenase gene expression”. Bioscience, Biotechnology, and Biochemistry. 70 (2): 401\u201310. doi:10.1271\/bbb.70.401. PMID\u00a016495656. S2CID\u00a025853385.Huh JW, Robinson RC, Lee HS, Lee JI, Heo YS, Kim HT, Lee HJ, Cho SW, Choe H (2006). “Expression, purification, crystallization, and preliminary X-Ray analysis of the human UDP-glucose dehydrogenase”. Protein and Peptide Letters. 13 (8): 859\u201362. doi:10.2174\/092986606777841253. PMID\u00a017073734. S2CID\u00a028298102.Easley KE, Sommer BJ, Boanca G, Barycki JJ, Simpson MA (Jan 2007). “Characterization of human UDP-glucose dehydrogenase reveals critical catalytic roles for lysine 220 and aspartate 280”. Biochemistry. 46 (2): 369\u201378. doi:10.1021\/bi061537d. PMID\u00a017209547.       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