Glucose-fructose oxidoreductase, a periplasmic enzyme of Zymomonas mobilis, is active in its precursor form |
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Authors: | H. Loos H. Sahm G.A. Sprenger |
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Affiliation: | Institut für Biotechnologie 1, Forschungszentrum Jülich GmbH, Jülich, FRG |
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Abstract: | Abstract Glucose-fructose oxidoreductase (GFOR) is a periplasmic enzyme of the ethanologenic, Gram-negative bacterium Zymomonas mobilis . It contains tightly bound NADP+ as cofactor. In Z. mobilis GFOR-recombinant strains, a precursor form of GFOR was accumulated. To assay the preGFOR for its NADP(H) content and enzymatic activity, it was purified from an overproducing strain. Using SDS-PAGE, the precursor subunit size was determined to approximately 45 kDa (compared with a 40 kDa subunit size for the mature GFOR subunit). The N-terminal amino acid sequence of the precursor was determined. The N-terminal residues of the GFOR matched with the signal sequence from the DNA sequence of the gene gfo . The precursor form of GFOR was enzymatically active and contained the cofactor NADP(H). |
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Keywords: | Zymomonas mobilis Glucose-fructose oxidoreductase Precursor form NADP(H) cofactor Activity stain |
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