UGDH
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesUGDH, GDH, UDP-GlcDH, UDPGDH, UGD, UDP-glucose 6-dehydrogenase, EIEE84, DEE84
External IDsOMIM: 603370 MGI: 1306785 HomoloGene: 2520 GeneCards: UGDH
Orthologs
SpeciesHumanMouse
Entrez

7358

22235

Ensembl

ENSG00000109814

ENSMUSG00000029201

UniProt

O60701

O70475

RefSeq (mRNA)

NM_001184700
NM_001184701
NM_003359

NM_009466

RefSeq (protein)

NP_001171629
NP_001171630
NP_003350

NP_033492

Location (UCSC)Chr 4: 39.5 – 39.53 MbChr 5: 65.57 – 65.59 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

UDP-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]

Nomenclature

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, and
  • uridine diphosphate D-glucose dehydrogenase.

Biochemistry

UDP-glucose 6-dehydrogenase
Identifiers
EC no.1.1.1.22
CAS no.9028-26-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a UDP-glucose 6-dehydrogenase (EC 1.1.1.22) is an enzyme that catalyzes the chemical reaction

UDP-glucose + 2 NAD+ + H2O 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

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000109814 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029201 - 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. 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): 25117–24. doi:10.1074/jbc.273.39.25117. PMID 9737970.
  6. 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 (3–4): 244–5. doi:10.1159/000015350. PMID 10575217. S2CID 25740995.
  7. 1 2 "Entrez Gene: UGDH UDP-glucose dehydrogenase".
  8. Hengel, H., Bosso-Lefèvre, 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
  9. Druzhinina TN, Kusov YY, Shibaev VN, Kochetkov NK, Bielý P, Kucár S, Bauer S (Feb 1975). "Uridine diphosphate 2-deoxyglucose. Chemical synthesis, enzymic oxidation and epimerization". Biochimica et Biophysica Acta. 381 (2): 301–7. doi:10.1016/0304-4165(75)90236-6. PMID 1091296.
  10. Kalckar HM, Maxwell ES, Strominger JL (Nov 1956). "Some properties of uridine diphosphoglucose dehydrogenase". Archives of Biochemistry and Biophysics. 65 (1): 2–10. doi:10.1016/0003-9861(56)90171-0. PMID 13373402.
  11. Strominger JL, Mapson LW (Aug 1957). "Uridine diphosphoglucose dehydrogenase of pea seedlings". The Biochemical Journal. 66 (4): 567–72. doi:10.1042/bj0660567. PMC 1200063. PMID 13459898.
  12. Axelrod J, Kalckar HM, Maxwell ES, Strominger JL (Jan 1957). "Enzymatic formation of uridine diphosphoglucuronic acid". The Journal of Biological Chemistry. 224 (1): 79–90. doi:10.1016/S0021-9258(18)65012-4. PMID 13398389.

Further reading

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