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Gene Review:

ECs0128 - glucose dehydrogenase

Escherichia coli O157:H7 str. Sakai

Persson, M. et al., Muramatsu, H. et al., Olsthoorn, A.J. et al., Uwajima, T. et al., Sanchez-Weatherby, J. et al., et al.

Woodward, Mattingly, Danson, Hough, Ward, Adams,

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Disease relevance of ECs0128

Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41 [1].
The gene encoding glucose dehydrogenase (EC 1.1.1.47) from Bacillus subtilis was inserted in a plasmid 1.0 kb downstream from a lac promoter, resulting in a 70-fold higher production of the enzyme when expressed in Escherichia coli [2].
After reduction of folate with zinc, dihydrofolate was reduced asymmetrically to (6)-tetra-hydrofolate by use of dihydrofolate reductase from E. coli C600/pTP600, with simultaneous NADPH cofactor recycling using glucose dehydrogenase from Gluconobacter scleroideus KY3613 [3].

High impact information on ECs0128

The reaction is based on the oxidation of glucose by Thermoplasma acidophilum glucose dehydrogenase with the concomitant oxidation of NADPH by Pyrococcus furiosus hydrogenase [4].
The predicted amino acid sequence shows significant homology with four flavin proteins: choline dehydrogenase, a glucose dehydrogenase and two oxidases [5].
A glucose dehydrogenase mutant containing a cysteine residue at position 44 could also be expressed at the same high level [2].
The apoform of D-glucose dehydrogenase from E. coli is reconstituted with pyrroloquinoline quinone to the holoenzyme in the presence of Mg2+ and assayed for glucose dehydrogenase activity [6].
The soluble quinoprotein glucose dehydrogenase oxidizes glucose, maltose and a variety of other monosaccharides and disaccharides to the corresponding lactones [7].

Chemical compound and disease context of ECs0128

Soluble, periplasmic quinoprotein glucose dehydrogenase of Acinetobacter calcoaceticus (sGDH; EC 1.1.99.17) was produced in good yield in the apoenzyme form (without the cofactor pyrroloquinoline quinone, PQQ) by an Escherichia coli recombinant strain provided with a plasmid containing the gene under control of a lac promoter [8].
An enzymatic system for the synthesis of L-pipecolic acid from L-lysine by commercial L-lysine alpha-oxidase from Trichoderma viride and an extract of recombinant Escherichia coli cells coexpressing Delta(1)-piperideine-2-carboxylate reductase from Pseudomonas putida and glucose dehydrogenase from Bacillus subtilis is described [9].

Analytical, diagnostic and therapeutic context of ECs0128

Purification and site-specific immobilization of genetically engineered glucose dehydrogenase on thiopropyl-Sepharose [2].
Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding [7].

References

Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41. Dokter, P., Frank, J., Duine, J.A. Biochem. J. (1986) [Pubmed]
Purification and site-specific immobilization of genetically engineered glucose dehydrogenase on thiopropyl-Sepharose. Persson, M., Bülow, L., Mosbach, K. FEBS Lett. (1990) [Pubmed]
Chemo-enzymatic synthesis of optically pure l-leucovorin, an augmentor of 5-fluorouracil cytotoxicity against cancer. Uwajima, T., Oshiro, T., Eguchi, T., Kuge, Y., Horiguchi, A., Igarashi, A., Mochida, K., Iwakura, M. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
In vitro hydrogen production by glucose dehydrogenase and hydrogenase. Woodward, J., Mattingly, S.M., Danson, M., Hough, D., Ward, N., Adams, M. Nat. Biotechnol. (1996) [Pubmed]
DNA sequence determination and functional characterization of the OCT-plasmid-encoded alkJKL genes of Pseudomonas oleovorans. van Beilen, J.B., Eggink, G., Enequist, H., Bos, R., Witholt, B. Mol. Microbiol. (1992) [Pubmed]
Enzymatic determination of pyrroloquinoline quinone using crude membranes from Escherichia coli. Geiger, O., Görisch, H. Anal. Biochem. (1987) [Pubmed]
Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding. Sanchez-Weatherby, J., Southall, S., Oubrie, A. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
Production, characterization, and reconstitution of recombinant quinoprotein glucose dehydrogenase (soluble type; EC 1.1.99.17) apoenzyme of Acinetobacter calcoaceticus. Olsthoorn, A.J., Duine, J.A. Arch. Biochem. Biophys. (1996) [Pubmed]
Enzymatic Synthesis of L-Pipecolic Acid by Delta(1)-Piperideine-2-carboxylate Reductase from Pseudomonas putida. Muramatsu, H., Mihara, H., Yasuda, M., Ueda, M., Kurihara, T., Esaki, N. Biosci. Biotechnol. Biochem. (2006) [Pubmed]

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