Skip to main content
The Journal of Biological Chemistry logoLink to The Journal of Biological Chemistry
. 2013 Oct 18;288(42):30502. doi: 10.1074/jbc.A111.248690

Characterization of a novel β-l-arabinofuranosidase in Bifidobacterium longum. FUNCTIONAL ELUCIDATION OF A DUF1680 FAMILY MEMBER.

Kiyotaka Fujita, Yukari Takashi, Eriko Obuchi, Kanefumi Kitahara, Toshihiko Suganuma
PMCID: PMC3798514  PMID: 24143008

VOLUME 286 (2011) PAGES 38079–38085

This article has been withdrawn by the authors.

In the original manuscript, the results of E338A and E366A mutants were reversed. We transformed Escherichia coli BL21 (λDE3) cells with the E366A plasmid instead of the E338A plasmid when sample tubes were switched inadvertently. The correct E338A and E366A mutants were expressed, purified, and characterized again. The results showed that Glu-338, and not Glu-366, is critical for catalytic activity. We wish to withdraw the manuscript and submit a corrected manuscript. We apologize for any inconvenience caused by this error.


Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology

RESOURCES