Biology:UDP-glucose 6-dehydrogenase

From HandWiki
Short description: Mammalian protein found in humans


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example


UDP-glucose 6-dehydrogenase is a cytosolic enzyme that in humans is encoded by the UGDH gene.[1][2][3]

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.[3]

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[4]

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 number1.1.1.22
CAS number9028-26-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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 [math]\displaystyle{ \rightleftharpoons }[/math] 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:[5][6][7][8]

References

  1. ↑ "Molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes". The Journal of Biological Chemistry 273 (39): 25117–24. Sep 1998. doi:10.1074/jbc.273.39.25117. PMID 9737970. 
  2. ↑ "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. Jan 2000. doi:10.1159/000015350. PMID 10575217. 
  3. ↑ 3.0 3.1 "Entrez Gene: UGDH UDP-glucose dehydrogenase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7358. 
  4. ↑ 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
  5. ↑ "Uridine diphosphate 2-deoxyglucose. Chemical synthesis, enzymic oxidation and epimerization". Biochimica et Biophysica Acta 381 (2): 301–7. Feb 1975. doi:10.1016/0304-4165(75)90236-6. PMID 1091296. 
  6. ↑ "Some properties of uridine diphosphoglucose dehydrogenase". Archives of Biochemistry and Biophysics 65 (1): 2–10. Nov 1956. doi:10.1016/0003-9861(56)90171-0. PMID 13373402. 
  7. ↑ "Uridine diphosphoglucose dehydrogenase of pea seedlings". The Biochemical Journal 66 (4): 567–72. Aug 1957. doi:10.1042/bj0660567. PMID 13459898. 
  8. ↑ "Enzymatic formation of uridine diphosphoglucuronic acid". The Journal of Biological Chemistry 224 (1): 79–90. Jan 1957. doi:10.1016/S0021-9258(18)65012-4. PMID 13398389. 

Further reading

  • "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): 166–72. Oct 1998. PMID 9850599. 
  • "Human UDP-glucose dehydrogenase gene: complete cloning and transcription start mapping". Biochemical and Biophysical Research Communications 275 (3): 981–5. Sep 2000. doi:10.1006/bbrc.2000.3389. PMID 10973831. 
  • "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): 21566–75. Jun 2003. doi:10.1074/jbc.M209366200. PMID 12682078. 
  • "Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive oxidations". The Journal of Biological Chemistry 279 (22): 23590–6. May 2004. doi:10.1074/jbc.M401928200. PMID 15044486. 
  • "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology 22 (6): 707–16. Jun 2004. doi:10.1038/nbt971. PMID 15146197. 
  • "Importance of Gly-13 for the coenzyme binding of human UDP-glucose dehydrogenase". The Journal of Biological Chemistry 279 (36): 37491–8. Sep 2004. doi:10.1074/jbc.M404234200. PMID 15247292. 
  • "Identification of a UDP-glucose-binding site of human UDP-glucose dehydrogenase by photoaffinity labeling and cassette mutagenesis". Bioconjugate Chemistry 16 (3): 710–6. 2005. doi:10.1021/bc0500387. PMID 15898741. 
  • "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): 703–9. Jun 2005. doi:10.1093/jb/mvi082. PMID 16002992. 
  • "A two-dimensional electrophoresis reference map of human ovary". Journal of Molecular Medicine 83 (10): 812–21. Oct 2005. doi:10.1007/s00109-005-0676-y. PMID 16021519. 
  • "Identification of a cis-acting element responsible for negative regulation of the human UDP-glucose dehydrogenase gene expression". Bioscience, Biotechnology, and Biochemistry 70 (2): 401–10. Feb 2006. doi:10.1271/bbb.70.401. PMID 16495656. 
  • "Expression, purification, crystallization, and preliminary X-Ray analysis of the human UDP-glucose dehydrogenase". Protein and Peptide Letters 13 (8): 859–62. 2006. doi:10.2174/092986606777841253. PMID 17073734. 
  • "Characterization of human UDP-glucose dehydrogenase reveals critical catalytic roles for lysine 220 and aspartate 280". Biochemistry 46 (2): 369–78. Jan 2007. doi:10.1021/bi061537d. PMID 17209547. 



Retrieved from "https://handwiki.org/wiki/index.php?title=Biology:UDP-glucose_6-dehydrogenase&oldid=3550492"