Correction: Author Correction: Improving 10-deacetylbaccatin III-10-β-O-acetyltransferase catalytic fitness for Taxol production

Abstract

Nature Communications 8: Article number: 15544 (2017); Published: 18 May 2017, Updated: 13 July 2018 In the originally published version of this Article, financial support was not fully acknowledged. The PDF and HTML versions of the Article have now been corrected to include support from the National Natural Science Foundation of China grant number 81573325.

Establishment of a Novel Cell Surface Display Platform Based on Natural “Chitosan Beads” of Yeast Spores

“…To demonstrate the practicability of this surface display system, a β-xylosidase named LXYL-P1-2, which is involved in the key reaction step for the production of paclitaxel, was selected. LXYL-P1-2 catalyzes the conversion of 7-β-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT) by releasing the D-xylosyl group at the C-7 position, and DT can be further converted to paclitaxel by an acetyltransferase . As a tetrameric macromolecular protein, LXYL-P1-2 has 10 glycosylation sites, and the molecular weight is approximately 110 kDa after glycosylation (Figure A).…”

“…LXYL-P1-2 catalyzes the conversion of 7-β-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT) by releasing the D-xylosyl group at the C-7 position, and DT can be further converted to paclitaxel by an acetyltransferase. 52 As a tetrameric macromolecular protein, 53 LXYL-P1-2 has 10 glycosylation sites, and the molecular weight is approximately 110 kDa after glycosylation (Figure 4A). To date, the cell surface display of LXYL-P1-2 in microorganisms has not been achieved because of its high molecular weight and complicated structure.…”