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Gene Review:

UGDH - UDP-glucose 6-dehydrogenase

Bos taurus

Lind, T. et al., Alary, J. et al., De Luca, G. et al., Drake, R.R. et al., Ordman, A.B. et al., et al.

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High impact information on UGDH

Photoincorporation of [beta-32P]5-N3UDP-GlcA into bovine liver UDP-Glc dehydrogenase (EC 1.1.1.22) was saturable with an apparent Kd of 12.5 microM, and was inhibited by the known active-site effectors UDP-GlcA, UDP-Glc, and UDP-xylose [1].
The oxidation of UDP-glucose by the enzyme UDP-glucose dehydrogenase (EC 1.1.1.22) from beef liver has been shown to proceed via the enzyme-bound intermediate, UDP-alpha-D-glyco-hexodialdose [2].
The catalytic-site thiol groups of UDP-glucose dehydrogenase from bovine liver were carboxymethylated with iodo[2-14C]acetate or with iodoacetamidofluorescein [3].
[After submission of the manuscript, a study appeared describing the molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes (Spicer et al., 1998).] The enzyme catalyzes the conversion of UDP-glucose to UDP-glucuronic acid, an essential precursor in glycosaminoglycan biosynthesis [4].
We have isolated a cDNA encoding UDP-glucose dehydrogenase from a bovine kidney cDNA-library, the first mammalian cDNA clone published [4].

Anatomical context of UGDH

Expression of the enzyme in COS-7 cells showed a 3-fold increase in UDP-glucose dehydrogenase activity; also, the C-terminal 23 amino acids was shown not to be necessary for enzyme activity [4].
Cadmium did not increase the breakdown of UDPGA by microsomal UDPGA pyrophosphatase but strongly decreased (30-66%) the synthesis of the cofactor in the cytosol by inhibiting UDP-glucose dehydrogenase (UDPGDH) [5].

Associations of UGDH with chemical compounds

Both in vitro and in vivo results support the conclusion that in intact cells the reduction in overall 4-OHCIPC glucuronidation caused by cadmium was due to a decrease in UDPGA availability which results from the inhibiting effect of cadmium on UDPGDH [5].
Overexpression, one-step purification and characterization of UDP-glucose dehydrogenase and UDP-N-acetylglucosamine pyrophosphorylase [6].
The physiological meaning of UDP-glucose 4'-epimerase in glycosaminoglycan biosynthesis in the two tissues under study is discussed on the basis of the Km values of UDP-glucose 4'-epimerase and UDP-glucose dehydrogenase and on the basis of the rate of UDP-glucose and UDP-galactose utilization [7].

Analytical, diagnostic and therapeutic context of UGDH

Purification of UDP-glucose dehydrogenase by hydrophobic and affinity chromatography [8].

References

Synthesis and characterization of 5-azido-UDP-glucuronic acid. A new photoaffinity probe for UDP-glucuronic acid-utilizing proteins. Drake, R.R., Zimniak, P., Haley, B.E., Lester, R., Elbein, A.D., Radominska, A. J. Biol. Chem. (1991) [Pubmed]
Mechanism of action of uridine diphoglucose dehydrogenase. Evidence for an essential lysine residue at the active site. Ordman, A.B., Kirkwood, S. J. Biol. Chem. (1977) [Pubmed]
Amino acid sequence of the tryptic peptide containing the catalytic-site thiol group of bovine liver uridine diphosphate glucose dehydrogenase. Franzen, B., Carrubba, C., Feingold, D.S., Ashcom, J., Franzen, J.S. Biochem. J. (1981) [Pubmed]
cDNA cloning and expression of UDP-glucose dehydrogenase from bovine kidney. Lind, T., Falk, E., Hjertson, E., Kusche-Gullberg, M., Lidholt, K. Glycobiology (1999) [Pubmed]
Mechanism of cadmium-decreased glucuronidation in the rat. Alary, J., Cravedi, J.P., Baradat, M., Carrera, G. Biochem. Pharmacol. (1992) [Pubmed]
Overexpression, one-step purification and characterization of UDP-glucose dehydrogenase and UDP-N-acetylglucosamine pyrophosphorylase. De Luca, C., Lansing, M., Crescenzi, F., Martini, I., Shen, G.J., O'Regan, M., Wong, C.H. Bioorg. Med. Chem. (1996) [Pubmed]
Biosynthesis of glycosaminoglycans: uridine diphosphate glucose 4'-epimerase from cornea and epiphysial-plate cartilage. De Luca, G., Speziale, P., Balduini, C., Castellani, A.A. Connect. Tissue Res. (1975) [Pubmed]
Purification of UDP-glucose dehydrogenase by hydrophobic and affinity chromatography. Geren, C.R., Olomon, C.M., Primrose, D.C., Ebner, K.E. Prep. Biochem. (1977) [Pubmed]

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AgaP_AGAP006532	Anopheles gambiae str. PEST
AT5G15490	Arabidopsis thaliana
AT3G29360	Arabidopsis thaliana
AT5G39320	Arabidopsis thaliana
sqv-4	Caenorhabditis elegans
UGDH	Canis lupus familiaris
ugdh	Danio rerio
sgl	Drosophila melanogaster
UGDH	Gallus gallus
UGDH	Homo sapiens
UGDH	Macaca mulatta
Ugdh	Mus musculus
Os03g0604200	Oryza sativa Japonica Group
UGDH	Pan troglodytes
Ugdh	Rattus norvegicus
ugdh	Xenopus (Silurana) tropicalis

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