is essential for establishing an oxidative D-xylose catabolic pathway in Pseudomonas putida S12, but coexpression of the putative 2-keto-3-deoxy-D-xylonate dehydratase (XylX) improves the biomass yield by approximately 10%, while the growth rate is not altered. When XylA, catalyzing the next and final step in the pathway, is also coexpressed, both the biomass yield and the maximum growth rate increase. Lower-pathway activities of strains S12xylXD and S12xylD, which rely on endogenous semialdehyde dehydrogenase, are about one-half the activity of the strain that coexpresses the alpha-KGSA dehydrogenase (S12xylXAD)
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hanging-drop vapour-diffusion method at 20°C. Crystals that diffracted to 2.66 A resolution are obtained using sodium formate and polyethylene glycol 3350. They belong to space group C2, with unit-cell parameters a = 270.42, b = 236.13, c = 65.17 A, beta = 97.38°
PCR product cloned into pET19b. The resulting plasmid harvested from Escherichia coli JM109, sequenced, and transformed into Escherichia coli Rosetta(DE3)-pLysS expression strain. In-frame deletion mutant amplified and ligated into pTA131, sequenced, and transformed in Haloferax volcanii H26 DELTApyrE2
xylXABCD, xylXAD, xylXD, xylD or xylX ligated into the vector pJTmcs using the KpnI, XbaI, and XmaJI restriction sites, under the control of the constitutive tac promoter, expressed in Pseudomonas putida S12