UDP-Glucose Dehydrogenase

Strutural Characteristics
  • John Perozich
  • Amy Leksana
  • John Hempel
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 372)

Abstract

UDP-glucose dehydrogenase (UDPGDH; EC 1.1.1.22) belongs to a small family of NAD+-linked oxidoreductases which transfer four electrons per catalytic cycle. Other examples of four-electron-transferring enzymes include histidinol dehydrogenase, β-hy-droxy-ß-methylglutaryl-CoA reductase, and other nucleotide sugar dehydrogenases (Feingold and Franzen, 1981). The bovine liver enzyme is an apparent homohexamer of 52kDa subunits which appears to function as a trimer of dimers due to its half-sites reactivity to iodoacetate and iodoacetamide (Franzen et al., 1980). We have recently completed the first primary structure of UDPGDH from a mammalian source (bovine liver) (Hempel et al., 1994). Here we present additional details of the analysis and results of a search for potentially homologous proteins using profile analysis.

Keywords

Cysteine Aldehyde Lysine Pseudomonas Thiol 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Feingold, D. S., and Franzen, J. S., 1981, Pyridine mucleotide-linked four-electron transfer dehydrogenases, Trends Biochem. Sci. 6:103–106.CrossRefGoogle Scholar
  2. Franzen, B., Carruba, C., Feingold, D. S., Ashcom, J., and Franzen, J. S., 1981, Amino acid sequence of the tryptic peptide containing the catalytic-site thiol group of bovine liver uridine diphosphate glucose dehydrogenase, Biochem. J. 199:599–602.PubMedGoogle Scholar
  3. Franzen, J. S., Ashcom, J., Marchetti, P., Cardamone, J. J., and Feingold, D. S., 1980, Induced vs. preexisting asymmetry models for half-of-the-sites reactivity in bovine liver uridine diphosphoglucose dehydrogenase, Biochim. Biophys. Acta 614:242–255.PubMedCrossRefGoogle Scholar
  4. Gribskov, M., Lüthy, R., and Eisenberg, D., 1990, Profile analysis, Methods Enzymol. 183:146–159.PubMedGoogle Scholar
  5. Hempel, J., Perozich, J., Romovacek, H., Hinich, A., Kuo, I., and Feingold, D. S., 1994, UDP-glucose dehydrogenase from bovine liver: Primary structure and relationship to other dehydrogenases, Protein Sci. 3:1074–1080.PubMedCrossRefGoogle Scholar
  6. Nelsestuen, G. L., and Kirkwood, S., 1971, The mechanism of action of uridine diphosphoglucose dehydrogenase: Uridine diphosphodialdoses as intermediates, J. Biol. Chem. 246:3828–3834.Google Scholar
  7. Ordman, A. B., and Kirkwood, S., 1977, Mechanism of action of uridine diphosphoglucose dehydrogenase: Evidence for an essential lysine residue at the active site, J. Biol. Chem. 252:1320–1326.PubMedGoogle Scholar
  8. Pearson, W. R., and Lipman, D. J., 1988, Improved tools for biological sequence comparison, Proc. Natl. Acad. Sci. USA 85:2444–2448.PubMedCrossRefGoogle Scholar
  9. Riordan, J. F., McElvany, K. D., and Borders, C. L., 1977, Arginyl residues: Anion recognition sites in enzymes, Science 195:884–886.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • John Perozich
    • 1
  • Amy Leksana
    • 1
  • John Hempel
    • 1
  1. 1.Department of Molecular Genetics and BiochemistryUniversity of PittsburghPittsburghUSA

Personalised recommendations