Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli.

摘要: Pyruvate decarboxylase (EC 4.1.1.1) from Zymomonas mobilis purified to homogeneity by using dye-ligand and ion-exchange chromatography. Antibodies produced against the enzyme amino-terminal sequence obtained for pure were used select confirm identity of a genomic clone encoding selected library Z. DNA cloned into pUC9. The fragment expressed high levels pyruvate in Escherichia coli. Possible RNA polymerase ribosome-binding sites have been identified 59-untranslated region gene. Images